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Volumn , Issue , 2010, Pages 603-626

Proteomics in Pesticide Toxicology

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EID: 84882737183     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374367-1.00021-5     Document Type: Chapter
Times cited : (4)

References (227)
  • 1
    • 0034735782 scopus 로고    scopus 로고
    • Bacterial dehalorespiration with chlorinated benzenes
    • Adrian L., Szewzyk U., Wecke J., Görisch H. Bacterial dehalorespiration with chlorinated benzenes. Nature 2000, 408(6812):580-583.
    • (2000) Nature , vol.408 , Issue.6812 , pp. 580-583
    • Adrian, L.1    Szewzyk, U.2    Wecke, J.3    Görisch, H.4
  • 2
    • 38449091968 scopus 로고    scopus 로고
    • Identification of a chlorobenzene reductive dehalogenase in Dehalococcoides sp. strain CBDB1
    • Adrian L., Rahnenführer J., Gobom J., Hölscher T. Identification of a chlorobenzene reductive dehalogenase in Dehalococcoides sp. strain CBDB1. Appl. Environ. Microbiol. 2007, 73(23):7717-7724.
    • (2007) Appl. Environ. Microbiol. , vol.73 , Issue.23 , pp. 7717-7724
    • Adrian, L.1    Rahnenführer, J.2    Gobom, J.3    Hölscher, T.4
  • 3
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R., Mann M. Mass spectrometry-based proteomics. Nature 2003, 422(6928):198-207.
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 4
    • 65349083749 scopus 로고    scopus 로고
    • A high-resolution two dimensional Gel- and Pro-Q DPS-based proteomics workflow for phosphoprotein identification and quantitative profiling
    • Agrawal G.K., Thelen J.J. A high-resolution two dimensional Gel- and Pro-Q DPS-based proteomics workflow for phosphoprotein identification and quantitative profiling. Methods Mol. Biol. 2009, 527:3-19.
    • (2009) Methods Mol. Biol. , vol.527 , pp. 3-19
    • Agrawal, G.K.1    Thelen, J.J.2
  • 5
    • 33846298496 scopus 로고    scopus 로고
    • Response to (chloro)biphenyls of the polychlorobiphenyl-degrader Burkholderia xenovorans LB400 involves stress proteins also induced by heat shock and oxidative stress
    • Agulló L., Cámara B., Martínez P., Latorre V., Seeger M. Response to (chloro)biphenyls of the polychlorobiphenyl-degrader Burkholderia xenovorans LB400 involves stress proteins also induced by heat shock and oxidative stress. FEMS Microbiol. Lett. 2007, 267(2):167-175.
    • (2007) FEMS Microbiol. Lett. , vol.267 , Issue.2 , pp. 167-175
    • Agulló, L.1    Cámara, B.2    Martínez, P.3    Latorre, V.4    Seeger, M.5
  • 6
    • 55249108443 scopus 로고    scopus 로고
    • Glyphosate-induced oxidative stress in rice leaves revealed by proteomic approach
    • Ahsan N., Lee D.G., Lee K.W., Alam I., Lee S.H., Bahk J.D., Lee B.H. Glyphosate-induced oxidative stress in rice leaves revealed by proteomic approach. Plant Physiol. Biochem. 2008, 46(12):1062-1070.
    • (2008) Plant Physiol. Biochem. , vol.46 , Issue.12 , pp. 1062-1070
    • Ahsan, N.1    Lee, D.G.2    Lee, K.W.3    Alam, I.4    Lee, S.H.5    Bahk, J.D.6    Lee, B.H.7
  • 7
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis, two-dimensional difference gel electrophoresis incorporating a pooled internal standard.
    • Alban A., David S.O., Bjorkesten L., Andersson C., Sloge E., Lewis S., Currie I. A novel experimental design for comparative two-dimensional gel analysis, two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 2003, 3(1):36-44.
    • (2003) Proteomics , vol.3 , Issue.1 , pp. 36-44
    • Alban, A.1    David, S.O.2    Bjorkesten, L.3    Andersson, C.4    Sloge, E.5    Lewis, S.6    Currie, I.7
  • 9
    • 35349027222 scopus 로고    scopus 로고
    • Studies on the glutathione S-transferase proteome of adult Drosophila melanogaster: Responsiveness to chemical challenge.
    • Alias Z., Clark A.G. Studies on the glutathione S-transferase proteome of adult Drosophila melanogaster: Responsiveness to chemical challenge. Proteomics 2007, 7(19):3618-3628.
    • (2007) Proteomics , vol.7 , Issue.19 , pp. 3618-3628
    • Alias, Z.1    Clark, A.G.2
  • 10
    • 34248176336 scopus 로고    scopus 로고
    • Discovering robust protein biomarkers for disease from relative expression reversals in 2-D DIGE data.
    • Anderson T.J., Tchernyshyov I., Diez R., Cole R.N., Geman D., Dang C.V., Winslow R.L. Discovering robust protein biomarkers for disease from relative expression reversals in 2-D DIGE data. Proteomics 2007, 8:1197-1207.
    • (2007) Proteomics , vol.8 , pp. 1197-1207
    • Anderson, T.J.1    Tchernyshyov, I.2    Diez, R.3    Cole, R.N.4    Geman, D.5    Dang, C.V.6    Winslow, R.L.7
  • 12
    • 26044473127 scopus 로고    scopus 로고
    • Influence of Bt-transgenic pollen, Bt-toxin and protease inhibitor (SBTI) ingestion on development of the hypopharyngeal glands in honeybees.
    • Babendreier D., Kalberer N.M., Romeis J., Fluri P., Mulligan E., Bigler F. Influence of Bt-transgenic pollen, Bt-toxin and protease inhibitor (SBTI) ingestion on development of the hypopharyngeal glands in honeybees. Apidologie 2005, 36:585-594.
    • (2005) Apidologie , vol.36 , pp. 585-594
    • Babendreier, D.1    Kalberer, N.M.2    Romeis, J.3    Fluri, P.4    Mulligan, E.5    Bigler, F.6
  • 13
    • 15944377843 scopus 로고    scopus 로고
    • Proteomics in developmental toxicology
    • Barrier M., Mirkes P.E. Proteomics in developmental toxicology. Reprod. Toxicol. 2005, 19:291-304.
    • (2005) Reprod. Toxicol. , vol.19 , pp. 291-304
    • Barrier, M.1    Mirkes, P.E.2
  • 14
    • 0022621961 scopus 로고
    • Rapid assay for screening and characterizing microorganisms for the ability to degrade polychlorinated biphenyls
    • Bedard D.L., Unterman R., Bopp L.H., Brennan M.J., Haberl M.L., Johnson C. Rapid assay for screening and characterizing microorganisms for the ability to degrade polychlorinated biphenyls. Appl. Environ. Microbiol. 1986, 51:761-768.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 761-768
    • Bedard, D.L.1    Unterman, R.2    Bopp, L.H.3    Brennan, M.J.4    Haberl, M.L.5    Johnson, C.6
  • 15
    • 0036736631 scopus 로고    scopus 로고
    • Assimilatory detoxification of herbicides by Delftia acidovorans MC1: induction of two chlorocatechol 1,2-dioxygenases as a response to chemostress
    • Benndorf D., Babel W. Assimilatory detoxification of herbicides by Delftia acidovorans MC1: induction of two chlorocatechol 1,2-dioxygenases as a response to chemostress. Microbiology 2002, 148(Pt 9):2883-2888.
    • (2002) Microbiology , vol.148 , Issue.PART 9 , pp. 2883-2888
    • Benndorf, D.1    Babel, W.2
  • 16
    • 1942537141 scopus 로고    scopus 로고
    • Regulation of catabolic enzymes during long-term exposure of Delftia acidovorans MC1 to chlorophenoxy herbicides
    • Benndorf D., Davidson I., Babel W. Regulation of catabolic enzymes during long-term exposure of Delftia acidovorans MC1 to chlorophenoxy herbicides. Microbiology 2004, 150(Pt 4):1005-1014.
    • (2004) Microbiology , vol.150 , Issue.PART 4 , pp. 1005-1014
    • Benndorf, D.1    Davidson, I.2    Babel, W.3
  • 17
    • 33745062542 scopus 로고    scopus 로고
    • Pseudomonas putida KT2440 responds specifically to chlorophenoxy herbicides and their initial metabolites.
    • Benndorf D., Thiersch M., Loffhagen N., Kunath C., Harms H. Pseudomonas putida KT2440 responds specifically to chlorophenoxy herbicides and their initial metabolites. Proteomics 2006, 6(11):3319-3329.
    • (2006) Proteomics , vol.6 , Issue.11 , pp. 3319-3329
    • Benndorf, D.1    Thiersch, M.2    Loffhagen, N.3    Kunath, C.4    Harms, H.5
  • 19
    • 70350273412 scopus 로고    scopus 로고
    • Improving protein extraction and separation methods for investigating the metaproteome of anaerobic benzene communities within sediments. Biodegradation DOI: 10.1007/s10532-009-9261-3.
    • Benndorf, D., Vogt, C., Jehmlich, N., Schmidt, Y., Thomas, H., Woffendin, G., Shevchenko, A., Richnow, H. H., and von Bergen, M. (2009). Improving protein extraction and separation methods for investigating the metaproteome of anaerobic benzene communities within sediments. Biodegradation DOI: 10.1007/s10532-009-9261-3.
    • (2009)
    • Benndorf, D.1    Vogt, C.2    Jehmlich, N.3    Schmidt, Y.4    Thomas, H.5    Woffendin, G.6    Shevchenko, A.7    Richnow, H.H.8    von Bergen, M.9
  • 20
    • 0036787711 scopus 로고    scopus 로고
    • High-throughput global peptide proteomic analysis by combining stable isotope amino acid labeling and data-dependent multiplexed-MS/MS
    • Berger S.J., Lee S.W., Anderson G.A., Pasa-Toli L., Toli N., Shen Y., Zhao R., Smith R.D. High-throughput global peptide proteomic analysis by combining stable isotope amino acid labeling and data-dependent multiplexed-MS/MS. Anal. Chem. 2002, 74(19):4994-5000.
    • (2002) Anal. Chem. , vol.74 , Issue.19 , pp. 4994-5000
    • Berger, S.J.1    Lee, S.W.2    Anderson, G.A.3    Pasa-Toli, L.4    Toli, N.5    Shen, Y.6    Zhao, R.7    Smith, R.D.8
  • 21
    • 34547783954 scopus 로고    scopus 로고
    • Precise protein quantification based on peptide quantification using iTRAQ
    • Boehm A.M., Pütz S., Altenhöfer D., Sickmann A., Falk M. Precise protein quantification based on peptide quantification using iTRAQ. BMC Bioinform 2007, 21(8):214.
    • (2007) BMC Bioinform , vol.21 , Issue.8 , pp. 214
    • Boehm, A.M.1    Pütz, S.2    Altenhöfer, D.3    Sickmann, A.4    Falk, M.5
  • 22
    • 33744463383 scopus 로고    scopus 로고
    • Dearomatizing benzene ring reductases
    • Boll M. Dearomatizing benzene ring reductases. J. Mol. Microbiol. Biotechnol. 2005, 10(2-4):132-142.
    • (2005) J. Mol. Microbiol. Biotechnol. , vol.10 , Issue.2-4 , pp. 132-142
    • Boll, M.1
  • 23
    • 4444226798 scopus 로고    scopus 로고
    • Protein composition of Paracoccus denitrificans cells grown on various electron acceptors and in the presence of azide.
    • Bouchal P., Precechtelová P., Zdráhal Z., Kucera I. Protein composition of Paracoccus denitrificans cells grown on various electron acceptors and in the presence of azide. Proteomics 2004, 4(9):2662-2671.
    • (2004) Proteomics , vol.4 , Issue.9 , pp. 2662-2671
    • Bouchal, P.1    Precechtelová, P.2    Zdráhal, Z.3    Kucera, I.4
  • 25
    • 20044372385 scopus 로고    scopus 로고
    • Comprehensive proteomics in yeast using chromatographic fractionation, gas phase fractionation, protein gel electrophoresis, and isoelectric focusing.
    • Breci L., Hattrup E., Keeler M., Letarte J., Johnson R., Haynes P.A. Comprehensive proteomics in yeast using chromatographic fractionation, gas phase fractionation, protein gel electrophoresis, and isoelectric focusing. Proteomics 2005, 5(8):2018-2028.
    • (2005) Proteomics , vol.5 , Issue.8 , pp. 2018-2028
    • Breci, L.1    Hattrup, E.2    Keeler, M.3    Letarte, J.4    Johnson, R.5    Haynes, P.A.6
  • 28
    • 0141560824 scopus 로고    scopus 로고
    • Insect resistance to Bacillus thuringiensis: alterations in the Indianmeal moth larval gut proteome
    • Candas M., Loseva O., Oppert B., Kosaraju P., Bulla L.A. Insect resistance to Bacillus thuringiensis: alterations in the Indianmeal moth larval gut proteome. Mol. Cell. Proteomics 2003, 2(1):19-28.
    • (2003) Mol. Cell. Proteomics , vol.2 , Issue.1 , pp. 19-28
    • Candas, M.1    Loseva, O.2    Oppert, B.3    Kosaraju, P.4    Bulla, L.A.5
  • 29
    • 54349090860 scopus 로고    scopus 로고
    • Catabolic pathways and cellular responses of Pseudomonas putida P8 during growth on benzoate with a proteomics approach
    • Cao B., Loh K.-C. Catabolic pathways and cellular responses of Pseudomonas putida P8 during growth on benzoate with a proteomics approach. Biotechnol. Bioeng. 2008, 101:1297-1312.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 1297-1312
    • Cao, B.1    Loh, K.-C.2
  • 30
    • 27144505199 scopus 로고    scopus 로고
    • Proteomic analysis of grapevine (Vitis vinifera L.) tissues subjected to herbicide stress
    • Castro A.J., Carapito C., Zorn N., Magné C., Leize E. Van., Dorsselaer A., Clément C. Proteomic analysis of grapevine (Vitis vinifera L.) tissues subjected to herbicide stress. J. Exp. Bot. 2005, 56(421):2783-2795.
    • (2005) J. Exp. Bot. , vol.56 , Issue.421 , pp. 2783-2795
    • Castro, A.J.1    Carapito, C.2    Zorn, N.3    Magné, C.4    Leize, E.5    Dorsselaer, A.6    Clément, C.7
  • 31
    • 0032948126 scopus 로고    scopus 로고
    • 2D protein electrophoresis, can it be perfected?
    • Celis J.E., Gromov P. 2D protein electrophoresis, can it be perfected?. Curr. Opin. Biotechnol 1999, 10(1):16-21.
    • (1999) Curr. Opin. Biotechnol , vol.10 , Issue.1 , pp. 16-21
    • Celis, J.E.1    Gromov, P.2
  • 32
    • 30144444853 scopus 로고    scopus 로고
    • Bioinformatic methods to exploit mass spectrometric data for proteomic applications
    • Chalkley R.J., Hansen K.C., Baldwin M.A. Bioinformatic methods to exploit mass spectrometric data for proteomic applications. Methods Enzymol. 2005, 402:289-312.
    • (2005) Methods Enzymol. , vol.402 , pp. 289-312
    • Chalkley, R.J.1    Hansen, K.C.2    Baldwin, M.A.3
  • 33
    • 49049090526 scopus 로고    scopus 로고
    • Review of a current role of mass spectrometry for proteome research
    • Chen C.H. Review of a current role of mass spectrometry for proteome research. Anal. Chim. Acta 2008, 624(1):16-36.
    • (2008) Anal. Chim. Acta , vol.624 , Issue.1 , pp. 16-36
    • Chen, C.H.1
  • 35
    • 33750588336 scopus 로고    scopus 로고
    • Advances in plant proteomics
    • Chen S., Harmon A.C. Advances in plant proteomics. Proteomics 2006, 20:5504-5516.
    • (2006) Proteomics , vol.20 , pp. 5504-5516
    • Chen, S.1    Harmon, A.C.2
  • 37
    • 0034043397 scopus 로고    scopus 로고
    • Induction of stress shock proteins DnaK and GroEL by phenoxyherbicide 2,4-D in Burkholderia sp. YK-2 isolated from rice field
    • Cho Y.S., Park S.H., Kim C.K., Oh K.H. Induction of stress shock proteins DnaK and GroEL by phenoxyherbicide 2,4-D in Burkholderia sp. YK-2 isolated from rice field. Curr. Microbiol. 2000, 41:33-38.
    • (2000) Curr. Microbiol. , vol.41 , pp. 33-38
    • Cho, Y.S.1    Park, S.H.2    Kim, C.K.3    Oh, K.H.4
  • 38
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/- 10ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser K.R., Baker P.R., Burlingame A.L. Role of accurate mass measurement (+/- 10ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal. Chem. 1999, 71:2871-2882.
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.R.2    Burlingame, A.L.3
  • 39
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: matching proteins with tandem mass spectra
    • Craig R., Beavis R.C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics 2004, 20(9):1466-1467.
    • (2004) Bioinformatics , vol.20 , Issue.9 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 40
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • Cravatt B.F., Simon G.M., Yates J.R. The biological impact of mass-spectrometry-based proteomics. Nature 2007, 450(7172):991-1000.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates, J.R.3
  • 41
    • 23044493446 scopus 로고    scopus 로고
    • Using worms to better understand how Bacillus thuringiensis kills insects
    • Crickmore N. Using worms to better understand how Bacillus thuringiensis kills insects. Trends Microbiol. 2005, 13(8):347-350.
    • (2005) Trends Microbiol. , vol.13 , Issue.8 , pp. 347-350
    • Crickmore, N.1
  • 43
    • 28044450599 scopus 로고    scopus 로고
    • Growth substrate- and phase-specific expression of biphenyl, benzoate, and C1 metabolic pathways in Burkholderia xenovorans LB400
    • Denef V.J., Patrauchan M.A., Florizone C., Park J., Tsoi T.V., Verstraete W., Tiedje J.M., Eltis L.D. Growth substrate- and phase-specific expression of biphenyl, benzoate, and C1 metabolic pathways in Burkholderia xenovorans LB400. J. Bacteriol. 2005, 187(23):7996-8005.
    • (2005) J. Bacteriol. , vol.187 , Issue.23 , pp. 7996-8005
    • Denef, V.J.1    Patrauchan, M.A.2    Florizone, C.3    Park, J.4    Tsoi, T.V.5    Verstraete, W.6    Tiedje, J.M.7    Eltis, L.D.8
  • 44
    • 51349132896 scopus 로고    scopus 로고
    • The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions
    • Denny P., Hagen F.K., Hardt M., Liao L., Yan W., Arellanno M., et al. The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions. J. Proteome Res. 2008, 7(5):1994-2006.
    • (2008) J. Proteome Res. , vol.7 , Issue.5 , pp. 1994-2006
    • Denny, P.1    Hagen, F.K.2    Hardt, M.3    Liao, L.4    Yan, W.5    Arellanno, M.6
  • 46
    • 33645234384 scopus 로고    scopus 로고
    • Protein carbonylation and heat shock response in Ruditapes decussatus following p,p'-dichlorodiphenyldichloroethylene (DDE) exposure: a proteomic approach reveals that DDE causes oxidative stress
    • Dowling V., Hoarau P.C., Romeo M., O'Halloran J.van., Pelt F., O'Brien N., Sheehan D. Protein carbonylation and heat shock response in Ruditapes decussatus following p,p'-dichlorodiphenyldichloroethylene (DDE) exposure: a proteomic approach reveals that DDE causes oxidative stress. Aquat. Toxicol. 2006, 77(1):11-18.
    • (2006) Aquat. Toxicol. , vol.77 , Issue.1 , pp. 11-18
    • Dowling, V.1    Hoarau, P.C.2    Romeo, M.3    O'Halloran, J.V.4    Pelt, F.5    O'Brien, N.6    Sheehan, D.7
  • 47
    • 13444251413 scopus 로고    scopus 로고
    • DynaProt 2D: an advanced proteomic database for dynamic online access to proteomes and two-dimensional electrophoresis gels
    • Database Issue
    • Drews O., Görg A. DynaProt 2D: an advanced proteomic database for dynamic online access to proteomes and two-dimensional electrophoresis gels. Nucleic Acids Res. 2005, 33(database issue):D583-D587.
    • (2005) Nucleic Acids Res. , vol.33
    • Drews, O.1    Görg, A.2
  • 48
    • 0009501415 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis for proteome analysis
    • BIOS, Oxford, S.R. Pennington, M.J. Dunn (Eds.)
    • Dunn M.J., Görg A. Two-dimensional polyacrylamide gel electrophoresis for proteome analysis. Proteomics"From Protein Sequence to Function 2001, 43-63. BIOS, Oxford. S.R. Pennington, M.J. Dunn (Eds.).
    • (2001) Proteomics"From Protein Sequence to Function , pp. 43-63
    • Dunn, M.J.1    Görg, A.2
  • 49
    • 49449088930 scopus 로고    scopus 로고
    • Anaerobic biodegradation of aromatic hydrocarbons: pathways and prospects
    • Foght J. Anaerobic biodegradation of aromatic hydrocarbons: pathways and prospects. J. Mol. Microbiol. Biotechnol. 2008, 15:93-120.
    • (2008) J. Mol. Microbiol. Biotechnol. , vol.15 , pp. 93-120
    • Foght, J.1
  • 50
    • 23944455372 scopus 로고    scopus 로고
    • Peptide sequence tags for fast database search in mass-spectrometry
    • Frank A., Tanner S., Bafna V., Pevzner P. Peptide sequence tags for fast database search in mass-spectrometry. J. Proteome Res. 2005, 4(4):1287-1295.
    • (2005) J. Proteome Res. , vol.4 , Issue.4 , pp. 1287-1295
    • Frank, A.1    Tanner, S.2    Bafna, V.3    Pevzner, P.4
  • 51
    • 0024978195 scopus 로고
    • The QUEST system for quantitative analysis of two-dimensional gels
    • Garrels J.I. The QUEST system for quantitative analysis of two-dimensional gels. J. Biol. Chem. 1989, 264(9):5269-5282.
    • (1989) J. Biol. Chem. , vol.264 , Issue.9 , pp. 5269-5282
    • Garrels, J.I.1
  • 52
    • 34547129626 scopus 로고    scopus 로고
    • Role of a carboxylesterase in herbicide bioactivation in Arabidopsis thaliana
    • Gershater M.C., Cummins I., Edwards R. Role of a carboxylesterase in herbicide bioactivation in Arabidopsis thaliana. J. Biol. Chem. 2007, 282(29):21460-21466.
    • (2007) J. Biol. Chem. , vol.282 , Issue.29 , pp. 21460-21466
    • Gershater, M.C.1    Cummins, I.2    Edwards, R.3
  • 53
    • 0037050277 scopus 로고    scopus 로고
    • Characterization of genes homologous to the general stress-inducible gene gls24 in Enterococcus faecalis and Lactococcus lactis
    • Giard J.C., Verneuil N., Auffray Y., Hartke A. Characterization of genes homologous to the general stress-inducible gene gls24 in Enterococcus faecalis and Lactococcus lactis. FEMS Microbiol. Lett. 2002, 206:235-239.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 235-239
    • Giard, J.C.1    Verneuil, N.2    Auffray, Y.3    Hartke, A.4
  • 54
    • 70449622561 scopus 로고    scopus 로고
    • Media containing aromatic compounds induce peculiar proteins in Acinetobacter radioresistens, as revealed by proteome analysis
    • Giuffrida M.G., Pessione E., Mazzoli R., Dellavalle G., Barello C., Conti A., Giunta C. Media containing aromatic compounds induce peculiar proteins in Acinetobacter radioresistens, as revealed by proteome analysis. Electrophoresis 2001, 22(9):1705-1711.
    • (2001) Electrophoresis , vol.22 , Issue.9 , pp. 1705-1711
    • Giuffrida, M.G.1    Pessione, E.2    Mazzoli, R.3    Dellavalle, G.4    Barello, C.5    Conti, A.6    Giunta, C.7
  • 56
    • 0024119482 scopus 로고
    • Two-dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): Method, reproducibility and genetic aspects.
    • Görg A., Postel W., Domscheit A., Günther S. Two-dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): Method, reproducibility and genetic aspects. Electrophoresis 1988, 9(11):681-692.
    • (1988) Electrophoresis , vol.9 , Issue.11 , pp. 681-692
    • Görg, A.1    Postel, W.2    Domscheit, A.3    Günther, S.4
  • 59
    • 0035676769 scopus 로고    scopus 로고
    • Computational aspects of protein identification by mass spectrometry
    • Gras R., Muller M. Computational aspects of protein identification by mass spectrometry. Curr. Opin. Mol. Ther. 2001, 3(6):526-532.
    • (2001) Curr. Opin. Mol. Ther. , vol.3 , Issue.6 , pp. 526-532
    • Gras, R.1    Muller, M.2
  • 60
    • 0035800468 scopus 로고    scopus 로고
    • Bt toxin resistance from loss of a putative carbohydrate-modifying enzyme.
    • Griffitts J.S., Whitacre J.L., Stevens D.E., Aroian R.V. Bt toxin resistance from loss of a putative carbohydrate-modifying enzyme. Science 2001, 293(5531):860-864.
    • (2001) Science , vol.293 , Issue.5531 , pp. 860-864
    • Griffitts, J.S.1    Whitacre, J.L.2    Stevens, D.E.3    Aroian, R.V.4
  • 61
    • 17644372743 scopus 로고    scopus 로고
    • What it takes to get a herbicide's mode of action. Physionomics, a classical approach in a new complexion
    • Grossmann K. What it takes to get a herbicide's mode of action. Physionomics, a classical approach in a new complexion. Pest Manag. Sci. 2005, 61(5):423-431.
    • (2005) Pest Manag. Sci. , vol.61 , Issue.5 , pp. 423-431
    • Grossmann, K.1
  • 63
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S.P., Rist B., Gerber S.A., Turecek F., Gelb M.H., Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 17(10):994-999.
    • (1999) Nat. Biotechnol. , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 64
    • 61349103096 scopus 로고    scopus 로고
    • Identification of thioredoxin disulfide targets using a quantitative proteomics approach based on isotope-coded affinity tags
    • Hägglund P., Bunkenborg J., Maeda K., Svensson B. Identification of thioredoxin disulfide targets using a quantitative proteomics approach based on isotope-coded affinity tags. J. Proteome Res. 2008, 7(12):5270-5276.
    • (2008) J. Proteome Res. , vol.7 , Issue.12 , pp. 5270-5276
    • Hägglund, P.1    Bunkenborg, J.2    Maeda, K.3    Svensson, B.4
  • 66
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han D.K., Eng J., Zhou H., Aebersold R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 2001, 19(10):946-951.
    • (2001) Nat. Biotechnol. , vol.19 , Issue.10 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 68
    • 84934438018 scopus 로고    scopus 로고
    • Quantitative protein profiling by mass spectrometry using isotope-coded affinity tags
    • Haqqani A.S., Kelly J.F., Stanimirovic D.B. Quantitative protein profiling by mass spectrometry using isotope-coded affinity tags. Methods Mol. Biol. 2008, 439:225-240.
    • (2008) Methods Mol. Biol. , vol.439 , pp. 225-240
    • Haqqani, A.S.1    Kelly, J.F.2    Stanimirovic, D.B.3
  • 69
    • 0029795374 scopus 로고    scopus 로고
    • The bη-ketoadipate pathway and the biology of self-identity
    • Harwood C.S., Parales R.E. The bη-ketoadipate pathway and the biology of self-identity. Annu. Rev. Microbiol. 1996, 50:553-590.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 70
    • 0032466209 scopus 로고    scopus 로고
    • Anaerobic metabolism of aromatic compounds via the benzoyl-CoA pathway
    • Harwood C.S., Burchhard G., Herrmann H., Fuchs G. Anaerobic metabolism of aromatic compounds via the benzoyl-CoA pathway. FEMS Microbial. Rev. 1998, 22(5):439-458.
    • (1998) FEMS Microbial. Rev. , vol.22 , Issue.5 , pp. 439-458
    • Harwood, C.S.1    Burchhard, G.2    Herrmann, H.3    Fuchs, G.4
  • 71
    • 0031018959 scopus 로고    scopus 로고
    • Anaerobic metabolism of aromatic compounds
    • Heider J., Fuchs G. Anaerobic metabolism of aromatic compounds. Eur. J. Biochem. 1997, 243(3):577-596.
    • (1997) Eur. J. Biochem. , vol.243 , Issue.3 , pp. 577-596
    • Heider, J.1    Fuchs, G.2
  • 72
    • 0346936145 scopus 로고    scopus 로고
    • Proteome reference map of Pseudomonas putida strain KT2440 for genome expression profiling: distinct responses of KT2440 and Pseudomonas aeruginosa strain PAO1 to iron deprivation and a new form of superoxide dismutase
    • Heim S., Ferrer M., Heuer H., Regenhardt D., Nimtz M., Timmis K.N. Proteome reference map of Pseudomonas putida strain KT2440 for genome expression profiling: distinct responses of KT2440 and Pseudomonas aeruginosa strain PAO1 to iron deprivation and a new form of superoxide dismutase. Environ. Microbiol. 2003, 5(12):1257-1269.
    • (2003) Environ. Microbiol. , vol.5 , Issue.12 , pp. 1257-1269
    • Heim, S.1    Ferrer, M.2    Heuer, H.3    Regenhardt, D.4    Nimtz, M.5    Timmis, K.N.6
  • 73
    • 58149235290 scopus 로고    scopus 로고
    • Tools for interpreting large-scale protein profiling in microbiology
    • Hendrickson E.L., Lamont R.J., Hackett M. Tools for interpreting large-scale protein profiling in microbiology. J. Dental Res. 2008, 87(11):1004-1015.
    • (2008) J. Dental Res. , vol.87 , Issue.11 , pp. 1004-1015
    • Hendrickson, E.L.1    Lamont, R.J.2    Hackett, M.3
  • 74
    • 0038047148 scopus 로고    scopus 로고
    • Popitam: towards new heuristic strategies to improve protein identification from tandem mass spectrometry data.
    • Hernandez P., Gras R., Frey J., Appel R.D. Popitam: towards new heuristic strategies to improve protein identification from tandem mass spectrometry data. Proteomics 2003, 3(6):870-878.
    • (2003) Proteomics , vol.3 , Issue.6 , pp. 870-878
    • Hernandez, P.1    Gras, R.2    Frey, J.3    Appel, R.D.4
  • 75
    • 33644898528 scopus 로고    scopus 로고
    • Automated protein identification by tandem mass spectrometry: Issues and strategies
    • Hernandez P., Müller M., Appel R.D. Automated protein identification by tandem mass spectrometry: Issues and strategies. Mass Spec. Rev. 2006, 25(2):235-254.
    • (2006) Mass Spec. Rev. , vol.25 , Issue.2 , pp. 235-254
    • Hernandez, P.1    Müller, M.2    Appel, R.D.3
  • 76
    • 0345306716 scopus 로고    scopus 로고
    • Introducing Professor Wolfgang Schumann, microbial stress responses section editor
    • Hightower L.E. Introducing Professor Wolfgang Schumann, microbial stress responses section editor. Cell Stress Chaperones 2003, 8(3):205-206.
    • (2003) Cell Stress Chaperones , vol.8 , Issue.3 , pp. 205-206
    • Hightower, L.E.1
  • 77
    • 0031970012 scopus 로고    scopus 로고
    • Dehalobacter restrictus gen. nov. and sp. nov., a strictly anaerobic bacterium that reductively dechlorinates tetra- and trichloroethene in an anaerobic respiration
    • Holliger C., Hahn D., Harmsen H., Ludwig W., Schumacher W., Tindall B., Vazquez F., Weiss N., Zehnder A.J.B. Dehalobacter restrictus gen. nov. and sp. nov., a strictly anaerobic bacterium that reductively dechlorinates tetra- and trichloroethene in an anaerobic respiration. Arch. Microbiol. 1998, 169(4):313-321.
    • (1998) Arch. Microbiol. , vol.169 , Issue.4 , pp. 313-321
    • Holliger, C.1    Hahn, D.2    Harmsen, H.3    Ludwig, W.4    Schumacher, W.5    Tindall, B.6    Vazquez, F.7    Weiss, N.8    Zehnder, A.J.B.9
  • 78
    • 33748323084 scopus 로고    scopus 로고
    • Proteomic analysis of root meristems and the effects of acetohydroxyacid synthase-inhibiting herbicides in the root of Medicago truncatula
    • Holmes P., Farquharson R., Hall P.J., Rolfe B.G. Proteomic analysis of root meristems and the effects of acetohydroxyacid synthase-inhibiting herbicides in the root of Medicago truncatula. J. Proteome Res. 2006, 5(9):2076.
    • (2006) J. Proteome Res. , vol.5 , Issue.9 , pp. 2076
    • Holmes, P.1    Farquharson, R.2    Hall, P.J.3    Rolfe, B.G.4
  • 79
    • 64549159728 scopus 로고    scopus 로고
    • MS-specific noise model reveals the potential of iTRAQ in quantitative proteomics.
    • Hundertmark C., Fischer R., Reinl T., May S., Klawonn F., Jänsch L. MS-specific noise model reveals the potential of iTRAQ in quantitative proteomics. Bioinformatics 2009, 25(8):1004-1011.
    • (2009) Bioinformatics , vol.25 , Issue.8 , pp. 1004-1011
    • Hundertmark, C.1    Fischer, R.2    Reinl, T.3    May, S.4    Klawonn, F.5    Jänsch, L.6
  • 81
    • 42449084881 scopus 로고    scopus 로고
    • LC-MS-based procedures for monitoring of toxic organophosphorus compounds and verification of pesticide and nerve agent poisoning
    • John H. LC-MS-based procedures for monitoring of toxic organophosphorus compounds and verification of pesticide and nerve agent poisoning. Anal. Bioanal. Chem. 2008, 391(1):97-116.
    • (2008) Anal. Bioanal. Chem. , vol.391 , Issue.1 , pp. 97-116
    • John, H.1
  • 83
    • 34250629255 scopus 로고    scopus 로고
    • A proteomic approach to study Cry1Ac binding proteins and their alterations in resistant Heliothis virescens larvae.
    • Jurat-Fuentes J.L., Adang M.J. A proteomic approach to study Cry1Ac binding proteins and their alterations in resistant Heliothis virescens larvae. J. Invert. Pathol. 2007, 95(3):187-191.
    • (2007) J. Invert. Pathol. , vol.95 , Issue.3 , pp. 187-191
    • Jurat-Fuentes, J.L.1    Adang, M.J.2
  • 84
    • 0036374159 scopus 로고    scopus 로고
    • Enhanced detection and characterization of protocatechuate 3,4-dioxygenase in Acinetobacter lwoffii K24 by proteomics using a column separation
    • Kahng H.Y., Cho K., Kim S.J. Enhanced detection and characterization of protocatechuate 3,4-dioxygenase in Acinetobacter lwoffii K24 by proteomics using a column separation. Biochem. Biophys. Res. Commun. 2002, 295:903-909.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 903-909
    • Kahng, H.Y.1    Cho, K.2    Kim, S.J.3
  • 85
    • 57749183941 scopus 로고    scopus 로고
    • Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation
    • Kang R., Wan J., Arstikaitis P., Takahashi H., Huang K., Bailey A.O., et al. Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation. Nature 2008, 456:904-909.
    • (2008) Nature , vol.456 , pp. 904-909
    • Kang, R.1    Wan, J.2    Arstikaitis, P.3    Takahashi, H.4    Huang, K.5    Bailey, A.O.6
  • 86
    • 61849084174 scopus 로고    scopus 로고
    • Comparison of three commercially available DIGE analysis software packages, minimal user intervention in gel-based proteomics
    • Kang Y., Techanukul T., Mantalaris A., Nagy J.M. Comparison of three commercially available DIGE analysis software packages, minimal user intervention in gel-based proteomics. J. Proteome Res. 2009, 8(2):1077-1084.
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 1077-1084
    • Kang, Y.1    Techanukul, T.2    Mantalaris, A.3    Nagy, J.M.4
  • 88
    • 0344845100 scopus 로고    scopus 로고
    • Proteomic analysis for the benzoate degradation pathway in Acinetobacter sp. KS-1
    • Kim S.I., Song S.Y., Kim K.W. Proteomic analysis for the benzoate degradation pathway in Acinetobacter sp. KS-1. Res. Microbiol. 2003, 154:697-703.
    • (2003) Res. Microbiol. , vol.154 , pp. 697-703
    • Kim, S.I.1    Song, S.Y.2    Kim, K.W.3
  • 89
    • 2342666128 scopus 로고    scopus 로고
    • Proteomic analysis of Acinetobacter lwoffii K24 by 2-D gel electrophoresis and electrospray ionization quadrupole-time of flight mass spectrometry.
    • Kim E.A., Kim J.Y., Kim S.J., Park K.R., Chung H.J., Leem S.H., Kim S.I. Proteomic analysis of Acinetobacter lwoffii K24 by 2-D gel electrophoresis and electrospray ionization quadrupole-time of flight mass spectrometry. J. Microbiol. Methods 2004, 57(3):337-349.
    • (2004) J. Microbiol. Methods , vol.57 , Issue.3 , pp. 337-349
    • Kim, E.A.1    Kim, J.Y.2    Kim, S.J.3    Park, K.R.4    Chung, H.J.5    Leem, S.H.6    Kim, S.I.7
  • 90
    • 10644256477 scopus 로고    scopus 로고
    • Identification of proteins induced by polycyclic aromatic hydrocarbon in Mycobacterium vanbaalenii PYR-1 using two-dimensional polyacrylamide gel electrophoresis and de novo sequencing methods
    • Kim S.J., Jones R.C., Cha C.J., Kweon O., Edmondson R.D., Cerniglia C.E. Identification of proteins induced by polycyclic aromatic hydrocarbon in Mycobacterium vanbaalenii PYR-1 using two-dimensional polyacrylamide gel electrophoresis and de novo sequencing methods. Proteomics 2004, 4:3899-3908.
    • (2004) Proteomics , vol.4 , pp. 3899-3908
    • Kim, S.J.1    Jones, R.C.2    Cha, C.J.3    Kweon, O.4    Edmondson, R.D.5    Cerniglia, C.E.6
  • 91
    • 8744256465 scopus 로고    scopus 로고
    • Proteome analysis of Pseudomonas sp. K82 biodegradation pathways
    • Kim S.I., Kim J.Y., Yun S.H., Kim J.H., Leem S.H., Lee C. Proteome analysis of Pseudomonas sp. K82 biodegradation pathways. Proteomics 2004, 4(11):3610-3621.
    • (2004) Proteomics , vol.4 , Issue.11 , pp. 3610-3621
    • Kim, S.I.1    Kim, J.Y.2    Yun, S.H.3    Kim, J.H.4    Leem, S.H.5    Lee, C.6
  • 92
    • 34648822321 scopus 로고    scopus 로고
    • A proteomics strategy for the analysis of bacterial biodegradation pathways.
    • Kim S.I., Choi J.S., Kahng H.Y. A proteomics strategy for the analysis of bacterial biodegradation pathways. OMICS 2007, 3:280-294.
    • (2007) OMICS , vol.3 , pp. 280-294
    • Kim, S.I.1    Choi, J.S.2    Kahng, H.Y.3
  • 93
    • 33846251226 scopus 로고    scopus 로고
    • Complete and integrated pyrene degradation pathway in Mycobacterium vanbaalenii PYR-1 based on systems biology
    • Kim S.J., Kweon O., Jones R.C., Freeman J.P., Edmondson R.D., Cerniglia C.E. Complete and integrated pyrene degradation pathway in Mycobacterium vanbaalenii PYR-1 based on systems biology. J. Bacteriol. 2007, 189(2):464-472.
    • (2007) J. Bacteriol. , vol.189 , Issue.2 , pp. 464-472
    • Kim, S.J.1    Kweon, O.2    Jones, R.C.3    Freeman, J.P.4    Edmondson, R.D.5    Cerniglia, C.E.6
  • 94
    • 34548134129 scopus 로고    scopus 로고
    • Peptide mass fingerprinting- and 2-DE/MS-based analysis of the biodegradation potential for monocyclic aromatic hydrocarbons in Pseudomonas sp
    • Kim S.I., Park S.H., Kim J.W., Leem S.H., Shin D.J., Kim S.H., Lee D.H., Kahng H.Y. Peptide mass fingerprinting- and 2-DE/MS-based analysis of the biodegradation potential for monocyclic aromatic hydrocarbons in Pseudomonas sp. Biotechnol. Lett. 2007, 29:1475-1481.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 1475-1481
    • Kim, S.I.1    Park, S.H.2    Kim, J.W.3    Leem, S.H.4    Shin, D.J.5    Kim, S.H.6    Lee, D.H.7    Kahng, H.Y.8
  • 95
    • 33644540488 scopus 로고    scopus 로고
    • Analysis of aromatic catabolic pathways in Pseudomonas putida KT 2440 using a combined proteomic approach: 2-DE/MS and cleavable isotope-coded affinity tag analysis
    • Kim Y.H., Cho K., Yun S.H., Kim J.Y., Kwon K.H., Yoo J.S., Kim S.I. Analysis of aromatic catabolic pathways in Pseudomonas putida KT 2440 using a combined proteomic approach: 2-DE/MS and cleavable isotope-coded affinity tag analysis. Proteomics 2006, 6:1301-1318.
    • (2006) Proteomics , vol.6 , pp. 1301-1318
    • Kim, Y.H.1    Cho, K.2    Yun, S.H.3    Kim, J.Y.4    Kwon, K.H.5    Yoo, J.S.6    Kim, S.I.7
  • 96
    • 84882800737 scopus 로고    scopus 로고
    • Environmental Processes II"Soil Decontamination, Vol. 11b
    • (Ed.)(H.-J. Rehm, G. Reed, A. Pühler, and P. Stadler, eds.), Wiley-VCH, Weinheim
    • Klein, J. (Vol. Ed.) (2000). Environmental Processes II"Soil Decontamination, Vol. 11b. In "Biotechnology" (H.-J. Rehm, G. Reed, A. Pühler, and P. Stadler, eds.), Wiley-VCH, Weinheim.
    • (2000) Biotechnology
    • Klein, J.1
  • 97
    • 0041358749 scopus 로고    scopus 로고
    • Use of proteomics and physiological characteristics to elucidate ecotoxic effects of methyl tert-butyl ether in Pseudomonas putida KT2440.
    • Krayl M., Benndorf D., Loffhagen N., Babel W. Use of proteomics and physiological characteristics to elucidate ecotoxic effects of methyl tert-butyl ether in Pseudomonas putida KT2440. Proteomics 2003, 3(8):1544-1552.
    • (2003) Proteomics , vol.3 , Issue.8 , pp. 1544-1552
    • Krayl, M.1    Benndorf, D.2    Loffhagen, N.3    Babel, W.4
  • 98
    • 26444477503 scopus 로고    scopus 로고
    • A bioinformatics perspective on proteomics: Data storage, analysis, and integration
    • Kremer A., Schneider R., Terstappen G.C. A bioinformatics perspective on proteomics: Data storage, analysis, and integration. Biosci. Rep. 2005, 25(1-2):95-106.
    • (2005) Biosci. Rep. , vol.25 , Issue.1-2 , pp. 95-106
    • Kremer, A.1    Schneider, R.2    Terstappen, G.C.3
  • 100
    • 0037701540 scopus 로고    scopus 로고
    • Identification of pyrene-induced proteins in Mycobacterium sp. strain 6PY1: evidence for two ring-hydroxylating dioxygenases
    • Krivobok S., Kuony S., Meyer C., Louwagie M., Willison J.C., Jouanneau Y. Identification of pyrene-induced proteins in Mycobacterium sp. strain 6PY1: evidence for two ring-hydroxylating dioxygenases. J. Bacteriol. 2003, 185:3828-3841.
    • (2003) J. Bacteriol. , vol.185 , pp. 3828-3841
    • Krivobok, S.1    Kuony, S.2    Meyer, C.3    Louwagie, M.4    Willison, J.C.5    Jouanneau, Y.6
  • 101
    • 37049039722 scopus 로고    scopus 로고
    • Analysis of DIGE data using a linear mixed model allowing for protein-specific dye effects
    • Krogh M., Liu Y., Waldemarson S., Valastro B., James P. Analysis of DIGE data using a linear mixed model allowing for protein-specific dye effects. Proteomics 2007, 7(23):4235-4244.
    • (2007) Proteomics , vol.7 , Issue.23 , pp. 4235-4244
    • Krogh, M.1    Liu, Y.2    Waldemarson, S.3    Valastro, B.4    James, P.5
  • 104
    • 14544281667 scopus 로고    scopus 로고
    • Substrate-dependent regulation of anaerobic degradation pathways for toluene and ethylbenzene in a denitrifying bacterium, strain EbN1
    • Kühner S., Wöhlbrand L., Fritz I., Wruck W., Hultschig C., Hufnagel P., Kube M., Reinhardt R., Rabus R. Substrate-dependent regulation of anaerobic degradation pathways for toluene and ethylbenzene in a denitrifying bacterium, strain EbN1. J. Bacteriol. 2005, 187(4):1493-1503.
    • (2005) J. Bacteriol. , vol.187 , Issue.4 , pp. 1493-1503
    • Kühner, S.1    Wöhlbrand, L.2    Fritz, I.3    Wruck, W.4    Hultschig, C.5    Hufnagel, P.6    Kube, M.7    Reinhardt, R.8    Rabus, R.9
  • 105
    • 34547933313 scopus 로고    scopus 로고
    • Microbial remediation of nitro-aromatic compounds: an overview
    • Kulkarni M., Chaudhari A. Microbial remediation of nitro-aromatic compounds: an overview. J. Environ Manag 2007, 85:496-512.
    • (2007) J. Environ Manag , vol.85 , pp. 496-512
    • Kulkarni, M.1    Chaudhari, A.2
  • 106
    • 33644943635 scopus 로고    scopus 로고
    • Analysis of the proteome of Pseudomonas putida KT2440 grown on different sources of carbon and energy
    • Kurbatov L., Albrecht D., Herrmann H., Petruschka L. Analysis of the proteome of Pseudomonas putida KT2440 grown on different sources of carbon and energy. Environ. Microbiol. 2006, 8:466-478.
    • (2006) Environ. Microbiol. , vol.8 , pp. 466-478
    • Kurbatov, L.1    Albrecht, D.2    Herrmann, H.3    Petruschka, L.4
  • 107
    • 34347401651 scopus 로고    scopus 로고
    • A polyomic approach to elucidate the fluoranthene degradative pathway in Mycobacterium vanbaalenii PYR-1
    • Kweon O., Kim S.J., Jones R.C., Freeman J.P., Adjei M.D., Edmondson R.D., Cerniglia C.E. A polyomic approach to elucidate the fluoranthene degradative pathway in Mycobacterium vanbaalenii PYR-1. J. Bacteriol. 2007, 189:4635-4647.
    • (2007) J. Bacteriol. , vol.189 , pp. 4635-4647
    • Kweon, O.1    Kim, S.J.2    Jones, R.C.3    Freeman, J.P.4    Adjei, M.D.5    Edmondson, R.D.6    Cerniglia, C.E.7
  • 108
    • 33744986051 scopus 로고    scopus 로고
    • Proteome changes after metabolic engineering to enhance aerobic mineralization of cis-1,2-dichloroethylene
    • Lee J., Cao L., Ow S.Y., Barrios-Llerena M.E., Chen W., Wood T.K., Wright P.C. Proteome changes after metabolic engineering to enhance aerobic mineralization of cis-1,2-dichloroethylene. J. Proteome Res. 2006, 5:1388-1397.
    • (2006) J. Proteome Res. , vol.5 , pp. 1388-1397
    • Lee, J.1    Cao, L.2    Ow, S.Y.3    Barrios-Llerena, M.E.4    Chen, W.5    Wood, T.K.6    Wright, P.C.7
  • 109
    • 33747773878 scopus 로고    scopus 로고
    • Proteomic responses to formic acid on Ralstonia eutropha
    • Lee S.-E., Li Q.X., Yu J. Proteomic responses to formic acid on Ralstonia eutropha. Proteomics 2006, 6:4259-4268.
    • (2006) Proteomics , vol.6 , pp. 4259-4268
    • Lee, S.-E.1    Li, Q.X.2    Yu, J.3
  • 110
    • 34347391727 scopus 로고    scopus 로고
    • Fluoranthene metabolism and associated proteins in Mycobacterium sp. JS14
    • Lee S.-E., Seo J.S., Keum Y.-S., Lee K.-J., Li Q.X. Fluoranthene metabolism and associated proteins in Mycobacterium sp. JS14. Proteomics 2007, 7(12):2059-2069.
    • (2007) Proteomics , vol.7 , Issue.12 , pp. 2059-2069
    • Lee, S.-E.1    Seo, J.S.2    Keum, Y.-S.3    Lee, K.-J.4    Li, Q.X.5
  • 111
    • 63049102070 scopus 로고    scopus 로고
    • Diverse protein regulations on PHA formation in Ralstonia eutropha on short chain organic acids
    • Lee S.-E., Li Q.X., Yu J. Diverse protein regulations on PHA formation in Ralstonia eutropha on short chain organic acids. Int. J. Biol. Sci. 2009, 5:215-225.
    • (2009) Int. J. Biol. Sci. , vol.5 , pp. 215-225
    • Lee, S.-E.1    Li, Q.X.2    Yu, J.3
  • 112
    • 0344494027 scopus 로고    scopus 로고
    • Applications of affinity chromatography in proteomics
    • Lee W.C., Lee K.H. Applications of affinity chromatography in proteomics. Anal. Biochem. 2004, 324(1):1-10.
    • (2004) Anal. Biochem. , vol.324 , Issue.1 , pp. 1-10
    • Lee, W.C.1    Lee, K.H.2
  • 113
    • 44949226052 scopus 로고    scopus 로고
    • Genetically engineered plants and foods: A scientist's analysis of the issues (Part I)
    • Lemaux P.G. Genetically engineered plants and foods: A scientist's analysis of the issues (Part I). Annu. Rev. Plant Biol. 2008, 59:771-812.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 771-812
    • Lemaux, P.G.1
  • 114
    • 0344737959 scopus 로고    scopus 로고
    • Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry
    • Li X.J., Zhang H., Ranish J.A., Aebersold R. Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry. Anal. Chem. 2003, 75(23):6648-6657.
    • (2003) Anal. Chem. , vol.75 , Issue.23 , pp. 6648-6657
    • Li, X.J.1    Zhang, H.2    Ranish, J.A.3    Aebersold, R.4
  • 116
    • 0036468595 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis, recent advances in sample preparation, detection and quantitation
    • Lilley K.S., Razzaq A., Dupree P. Two-dimensional gel electrophoresis, recent advances in sample preparation, detection and quantitation. Curr. Opin. Chem. Biol. 2002, 6(1):46-50.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , Issue.1 , pp. 46-50
    • Lilley, K.S.1    Razzaq, A.2    Dupree, P.3
  • 117
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications.
    • Liska A.J., Shevchenko A. Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications. Proteomics 2003, 3(1):19-28.
    • (2003) Proteomics , vol.3 , Issue.1 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2
  • 118
    • 0029781901 scopus 로고    scopus 로고
    • Initial characterization of a reductive dehalogenase from desulfitobacterium chlororespirans Co23
    • Loffler F.E., Sanford R.A., Tiedje J.M. Initial characterization of a reductive dehalogenase from desulfitobacterium chlororespirans Co23. Appl. Environ. Microbiol. 1996, 62(10):3809-3813.
    • (1996) Appl. Environ. Microbiol. , vol.62 , Issue.10 , pp. 3809-3813
    • Loffler, F.E.1    Sanford, R.A.2    Tiedje, J.M.3
  • 119
    • 0037640029 scopus 로고    scopus 로고
    • Description of Sulfurospirillum halorespirans sp. nov., an anaerobic, tetrachloroethene-respiring bacterium, and transfer of Dehalospirillum multivorans to the genus Sulfurospirillum as Sulfurospirillum multivorans comb. nov
    • Luijten M.L.G.C., de Weert J., Smidt H., Boschker H.T.S., de Vos W.M., Schraa G., Stams A.J.M. Description of Sulfurospirillum halorespirans sp. nov., an anaerobic, tetrachloroethene-respiring bacterium, and transfer of Dehalospirillum multivorans to the genus Sulfurospirillum as Sulfurospirillum multivorans comb. nov. Int. J. Syst. Evol. Microbiol. 2003, 53:787-793.
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 787-793
    • Luijten, M.L.G.C.1    de Weert, J.2    Smidt, H.3    Boschker, H.T.S.4    de Vos, W.M.5    Schraa, G.6    Stams, A.J.M.7
  • 120
    • 0029161113 scopus 로고
    • Two-dimensional gel electrophoresis analysis of the response of Pseudomonas putida KT 2442 to 2-chlorophenol
    • Lupi C.G., Colangelo T., Mason C.A. Two-dimensional gel electrophoresis analysis of the response of Pseudomonas putida KT 2442 to 2-chlorophenol. Appl. Environ. Microbiol. 1995, 61:2863-2872.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2863-2872
    • Lupi, C.G.1    Colangelo, T.2    Mason, C.A.3
  • 121
    • 0036828724 scopus 로고    scopus 로고
    • Probability-based validation of protein identifications using a modified SEQUEST algorithm
    • MacCoss M.J., Wu C.C., Yates J.R. Probability-based validation of protein identifications using a modified SEQUEST algorithm. Anal. Chem. 2002, 74(21):5593-5599.
    • (2002) Anal. Chem. , vol.74 , Issue.21 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates, J.R.3
  • 122
    • 0346122950 scopus 로고    scopus 로고
    • A correlation algorithm for the automated quantitative analysis of shotgun proteomics data
    • MacCoss M.J., Wu C.C., Liu H., Sadygov R., Yates J.R. A correlation algorithm for the automated quantitative analysis of shotgun proteomics data. Anal. Chem. 2003, 75(24):6912-6921.
    • (2003) Anal. Chem. , vol.75 , Issue.24 , pp. 6912-6921
    • MacCoss, M.J.1    Wu, C.C.2    Liu, H.3    Sadygov, R.4    Yates, J.R.5
  • 124
    • 34547754608 scopus 로고    scopus 로고
    • Chlorobenzoate inhibits growth and induces stress proteins in the PCB-degrading bacterium Burkholderia xenovorans LB400
    • Martínez P., Agulló L., Hernández M., Seeger M. Chlorobenzoate inhibits growth and induces stress proteins in the PCB-degrading bacterium Burkholderia xenovorans LB400. Arch. Microbiol. 2007, 188(3):289-297.
    • (2007) Arch. Microbiol. , vol.188 , Issue.3 , pp. 289-297
    • Martínez, P.1    Agulló, L.2    Hernández, M.3    Seeger, M.4
  • 125
    • 0344622120 scopus 로고    scopus 로고
    • Isolation of a bacterium that reductively dechlorinates tetrachloroethene to ethene.
    • Maymó-Gatell X., Chien Y., Gossett J.M., Zinder S.H. Isolation of a bacterium that reductively dechlorinates tetrachloroethene to ethene. Science 1997, 276:156.
    • (1997) Science , vol.276 , pp. 156
    • Maymó-Gatell, X.1    Chien, Y.2    Gossett, J.M.3    Zinder, S.H.4
  • 126
    • 34250381193 scopus 로고    scopus 로고
    • Degradation of aromatic compounds by Acinetobacter radioresistens S13: growth characteristics on single substrates and mixtures
    • Mazzoli R., Pessione E., Giuffrida M.G., Fattori P., Barello C., Giunta C., Lindley N.D. Degradation of aromatic compounds by Acinetobacter radioresistens S13: growth characteristics on single substrates and mixtures. Arch. Microbiol. 2007, 188(1):55-68.
    • (2007) Arch. Microbiol. , vol.188 , Issue.1 , pp. 55-68
    • Mazzoli, R.1    Pessione, E.2    Giuffrida, M.G.3    Fattori, P.4    Barello, C.5    Giunta, C.6    Lindley, N.D.7
  • 127
    • 34948813038 scopus 로고    scopus 로고
    • Transcriptome analysis of Pseudomonas putida KT2440 harboring the completely sequenced IncP-7 plasmid pCAR1
    • Miyakoshi M., Shintani M., Terabayashi T., Kai S., Yamane H., Nojiri H. Transcriptome analysis of Pseudomonas putida KT2440 harboring the completely sequenced IncP-7 plasmid pCAR1. J. Bacteriol. 2007, 189(19):6849-6860.
    • (2007) J. Bacteriol. , vol.189 , Issue.19 , pp. 6849-6860
    • Miyakoshi, M.1    Shintani, M.2    Terabayashi, T.3    Kai, S.4    Yamane, H.5    Nojiri, H.6
  • 128
    • 0035133932 scopus 로고    scopus 로고
    • Differential expression of mycobacterial proteins following phagocytosis by macrophages
    • Monahan I.M., Betts J., Banerjee D.K., Butcher P.D. Differential expression of mycobacterial proteins following phagocytosis by macrophages. Microbiology 2001, 147:459-471.
    • (2001) Microbiology , vol.147 , pp. 459-471
    • Monahan, I.M.1    Betts, J.2    Banerjee, D.K.3    Butcher, P.D.4
  • 130
    • 58949092969 scopus 로고    scopus 로고
    • Proteomic analysis of Metarhizium anisopliae secretion in the presence of the insect pest Callosobruchus maculatus
    • Murad A.M., Noronha E.F., Miller R.N., Costa F.T., Pereira C.D., Mehta A., Caldas R.A., Franco O.L. Proteomic analysis of Metarhizium anisopliae secretion in the presence of the insect pest Callosobruchus maculatus. Microbiology 2008, 154(Pt 12):3766-3774.
    • (2008) Microbiology , vol.154 , Issue.PART 12 , pp. 3766-3774
    • Murad, A.M.1    Noronha, E.F.2    Miller, R.N.3    Costa, F.T.4    Pereira, C.D.5    Mehta, A.6    Caldas, R.A.7    Franco, O.L.8
  • 131
    • 61449243723 scopus 로고    scopus 로고
    • Quantitative profiling of polar cationic metabolites in human cerebrospinal fluid by reversed-phase nanoliquid chromatography/mass spectrometry
    • Myint K.T., Aoshima K., Tanaka S., Nakamura T., Oda Y. Quantitative profiling of polar cationic metabolites in human cerebrospinal fluid by reversed-phase nanoliquid chromatography/mass spectrometry. Anal. Chem. 2009, 81(3):1121-1129.
    • (2009) Anal. Chem. , vol.81 , Issue.3 , pp. 1121-1129
    • Myint, K.T.1    Aoshima, K.2    Tanaka, S.3    Nakamura, T.4    Oda, Y.5
  • 133
    • 21144442133 scopus 로고    scopus 로고
    • Phenylacetate catabolism in Rhodococcus sp. strain RHA1: a central pathway for degradation of aromatic compounds
    • Navarro-Llorens J.M., Patrauchan M.A., Stewart G.R., Davies J.E., Eltis L.D., Mohn W.W. Phenylacetate catabolism in Rhodococcus sp. strain RHA1: a central pathway for degradation of aromatic compounds. J. Bacteriol. 2005, 187(13):4497-4504.
    • (2005) J. Bacteriol. , vol.187 , Issue.13 , pp. 4497-4504
    • Navarro-Llorens, J.M.1    Patrauchan, M.A.2    Stewart, G.R.3    Davies, J.E.4    Eltis, L.D.5    Mohn, W.W.6
  • 134
    • 0036933705 scopus 로고    scopus 로고
    • Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440
    • Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A., et al. Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440. Environ. Microbiol. 2002, 4(12):799-808.
    • (2002) Environ. Microbiol. , vol.4 , Issue.12 , pp. 799-808
    • Nelson, K.E.1    Weinel, C.2    Paulsen, I.T.3    Dodson, R.J.4    Hilbert, H.5    Martins dos Santos, V.A.6
  • 135
    • 35348860923 scopus 로고    scopus 로고
    • Proteomics for the analysis of environmental stress responses in organisms
    • Nesatyy V.J., Suter M.J.-F. Proteomics for the analysis of environmental stress responses in organisms. Environ. Sci. Technol. 2007, 41:6891-6900.
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 6891-6900
    • Nesatyy, V.J.1    Suter, M.J.-F.2
  • 136
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975, 250(10):4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , Issue.10 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 137
    • 34447569328 scopus 로고    scopus 로고
    • Purification and characterization of a novel nitrile hydratase from Rhodococcus sp. RHA1
    • Okamoto S., Eltis L.D. Purification and characterization of a novel nitrile hydratase from Rhodococcus sp. RHA1. Mol. Microbiol. 2007, 65(3):828-838.
    • (2007) Mol. Microbiol. , vol.65 , Issue.3 , pp. 828-838
    • Okamoto, S.1    Eltis, L.D.2
  • 138
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong S.E., Mann M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 2006, 1(6):2650-2660.
    • (2006) Nat. Protoc. , vol.1 , Issue.6 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 139
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., Mann M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 2002, 1(5):376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 140
    • 33750600611 scopus 로고    scopus 로고
    • Proteome informatics I: Bioinformatics tools for processing experimental data
    • Palagi P.M., Hernandez P., Walther D., Appel R.D. Proteome informatics I: Bioinformatics tools for processing experimental data. Proteomics 2006, 6:5435-5444.
    • (2006) Proteomics , vol.6 , pp. 5435-5444
    • Palagi, P.M.1    Hernandez, P.2    Walther, D.3    Appel, R.D.4
  • 141
    • 66149097411 scopus 로고    scopus 로고
    • Database interrogation algorithms for identification of proteins in proteomic separations
    • Palagi P.M., Lisacek F., Appel R.D. Database interrogation algorithms for identification of proteins in proteomic separations. Methods Mol. Biol. 2009, 519:515-531.
    • (2009) Methods Mol. Biol. , vol.519 , pp. 515-531
    • Palagi, P.M.1    Lisacek, F.2    Appel, R.D.3
  • 142
    • 0037112383 scopus 로고    scopus 로고
    • Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry
    • Palmblad M., Ramström M., Markides K.E., Håkansson P., Bergquist J. Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry. Anal. Chem. 2002, 74(22):5826-5830.
    • (2002) Anal. Chem. , vol.74 , Issue.22 , pp. 5826-5830
    • Palmblad, M.1    Ramström, M.2    Markides, K.E.3    Håkansson, P.4    Bergquist, J.5
  • 143
    • 43849089302 scopus 로고    scopus 로고
    • Characterization of anaerobic catabolism of p-coumarate in Rhodopseudomonas palustris by integrating transcriptomics and quantitative proteomics
    • Pan C., Oda Y., Lankford P.K., Zhang B., Samatova N.F., Pelletier D.A., Harwood C.S., Hettich R.L. Characterization of anaerobic catabolism of p-coumarate in Rhodopseudomonas palustris by integrating transcriptomics and quantitative proteomics. Mol. Cell. Proteomics 2008, 7:938-948.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 938-948
    • Pan, C.1    Oda, Y.2    Lankford, P.K.3    Zhang, B.4    Samatova, N.F.5    Pelletier, D.A.6    Harwood, C.S.7    Hettich, R.L.8
  • 144
    • 55949087672 scopus 로고    scopus 로고
    • Comparison of the membrane subproteomes during growth of a new Pseudomonas strain on lysogeny broth medium, glucose, and phenol
    • Papasotiriou D.G., Markoutsa S., Meyer B., Papadioti A., Karas M., Tsiotis G. Comparison of the membrane subproteomes during growth of a new Pseudomonas strain on lysogeny broth medium, glucose, and phenol. J. Proteome Res. 2008, 7(10):4278-4288.
    • (2008) J. Proteome Res. , vol.7 , Issue.10 , pp. 4278-4288
    • Papasotiriou, D.G.1    Markoutsa, S.2    Meyer, B.3    Papadioti, A.4    Karas, M.5    Tsiotis, G.6
  • 145
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin D.J, Hojrup P., Bleasby A.J. Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 1993, 3(6):327-332.
    • (1993) Curr. Biol. , vol.3 , Issue.6 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 146
    • 75649113704 scopus 로고    scopus 로고
    • Proteomics in insecticide toxicology
    • Park B.S., Lee S.E. Proteomics in insecticide toxicology. Mol. Cell. Toxicol. 2007, 3:11-18.
    • (2007) Mol. Cell. Toxicol. , vol.3 , pp. 11-18
    • Park, B.S.1    Lee, S.E.2
  • 147
    • 33846990172 scopus 로고    scopus 로고
    • Characterization of beta-ketoadipate pathway from multi-drug resistance bacterium, Acinetobacter baumannii DU202 by proteomic approach
    • Park S.H., Kim J.W., Yun S.H., Leem S.H., Kahng H.Y., Kim S.I. Characterization of beta-ketoadipate pathway from multi-drug resistance bacterium, Acinetobacter baumannii DU202 by proteomic approach. J. Microbiol. 2006, 44(6):632-640.
    • (2006) J. Microbiol. , vol.44 , Issue.6 , pp. 632-640
    • Park, S.H.1    Kim, J.W.2    Yun, S.H.3    Leem, S.H.4    Kahng, H.Y.5    Kim, S.I.6
  • 148
    • 35648960618 scopus 로고    scopus 로고
    • Regulation of gene expression
    • Taylor & Francis, New York, L. Eggeling, M. Bott (Eds.)
    • Pátek M. Regulation of gene expression. Handbook of Corynebacterium glutamicum 2005, 81-98. Taylor & Francis, New York. L. Eggeling, M. Bott (Eds.).
    • (2005) Handbook of Corynebacterium glutamicum , pp. 81-98
    • Pátek, M.1
  • 150
    • 13244273462 scopus 로고    scopus 로고
    • Profiling of abundant proteins associated with dichlorodiphenyltrichloroethane resistance in Drosophila melanogaster.
    • Pedra J.H., Festucci-Buselli R.A., Sun W., Muir W.M., Scharf M.E., Pittendrigh B.R. Profiling of abundant proteins associated with dichlorodiphenyltrichloroethane resistance in Drosophila melanogaster. Proteomics 2005, 5(1):258-269.
    • (2005) Proteomics , vol.5 , Issue.1 , pp. 258-269
    • Pedra, J.H.1    Festucci-Buselli, R.A.2    Sun, W.3    Muir, W.M.4    Scharf, M.E.5    Pittendrigh, B.R.6
  • 152
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20(18):3551-3567.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 155
    • 35649025273 scopus 로고    scopus 로고
    • Comparative proteomes of Corynebacterium glutamicum grown on aromatic compounds revealed novel proteins involved in aromatic degradation and a clear link between aromatic catabolism and gluconeogenesis via fructose-1,6-bisphosphatase
    • Qi S.W., Chaudhry M.T., Zhang Y., Meng B., Huang Y., Zhao K.X., Poetsch A., Jiang C.Y., Liu S., Liu S.vJ. Comparative proteomes of Corynebacterium glutamicum grown on aromatic compounds revealed novel proteins involved in aromatic degradation and a clear link between aromatic catabolism and gluconeogenesis via fructose-1,6-bisphosphatase. Proteomics 2007, 7(20):3775-3787.
    • (2007) Proteomics , vol.7 , Issue.20 , pp. 3775-3787
    • Qi, S.W.1    Chaudhry, M.T.2    Zhang, Y.3    Meng, B.4    Huang, Y.5    Zhao, K.X.6    Poetsch, A.7    Jiang, C.Y.8    Liu, S.9    Liu, S.10
  • 157
    • 55749083826 scopus 로고    scopus 로고
    • Fully denaturing two-dimensional electrophoresis of membrane proteins: a critical update
    • Rabilloud T., Chevallet M., Luche S., Lelong C. Fully denaturing two-dimensional electrophoresis of membrane proteins: a critical update. Proteomics 2008, 8(19):3965-3973.
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 3965-3973
    • Rabilloud, T.1    Chevallet, M.2    Luche, S.3    Lelong, C.4
  • 158
    • 27644578460 scopus 로고    scopus 로고
    • Functional genomics of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1
    • Rabus R. Functional genomics of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1. Appl. Microbiol. Biotechnol. 2005, 68(5):580-587.
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , Issue.5 , pp. 580-587
    • Rabus, R.1
  • 160
    • 0036637687 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis analysis of protein production during growth of Pseudomonas putida F1 on toluene, phenol, and their mixture
    • Reardon K.F., Kim K.H. Two-dimensional electrophoresis analysis of protein production during growth of Pseudomonas putida F1 on toluene, phenol, and their mixture. Electrophoresis 2002, 23(14):2233-2241.
    • (2002) Electrophoresis , vol.23 , Issue.14 , pp. 2233-2241
    • Reardon, K.F.1    Kim, K.H.2
  • 162
    • 0030855956 scopus 로고    scopus 로고
    • Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase
    • Richins R.D., Kaneva I., Mulchandani A., Chen W. Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus
    • (1997) Nat. Biotechnol. , vol.15 , Issue.10 , pp. 984-987
    • Richins, R.D.1    Kaneva, I.2    Mulchandani, A.3    Chen, W.4
  • 163
    • 0141788463 scopus 로고    scopus 로고
    • Tissue-specific expression and localization of safener-induced glutathione S-transferase proteins in Triticum tauschii.
    • Riechers D.E., Zhang Q., Xu F., Vaughn K.C. Tissue-specific expression and localization of safener-induced glutathione S-transferase proteins in Triticum tauschii. Planta 2003, 217(5):831-840.
    • (2003) Planta , vol.217 , Issue.5 , pp. 831-840
    • Riechers, D.E.1    Zhang, Q.2    Xu, F.3    Vaughn, K.C.4
  • 165
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross P.L., Huang Y.N, Marchese J.N., Williamson B., Parker K., Hattan S., et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3:1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4    Parker, K.5    Hattan, S.6
  • 167
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: un amour impossible?
    • Santoni V., Molloy M., Rabilloud T. Membrane proteins and proteomics: un amour impossible?. Electrophoresis 2000, 21(6):1054-1070.
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 168
    • 4444316792 scopus 로고    scopus 로고
    • Insights into Pseudomonas putida KT2440 response to phenol-induced stress by quantitative proteomics
    • Santos P.M., Benndorf D., Sá-Correia I. Insights into Pseudomonas putida KT2440 response to phenol-induced stress by quantitative proteomics. Proteomics 2004, 4(9):2640-2652.
    • (2004) Proteomics , vol.4 , Issue.9 , pp. 2640-2652
    • Santos, P.M.1    Benndorf, D.2    Sá-Correia, I.3
  • 169
    • 34648827772 scopus 로고    scopus 로고
    • Mechanistic insights into the global response to phenol in the phenol-biodegrading strain Pseudomonas sp. M1 revealed by quantitative proteomics
    • Santos P.M., Roma V., Benndorf D., von Bergen M., Harm H., Sá-Correia I. Mechanistic insights into the global response to phenol in the phenol-biodegrading strain Pseudomonas sp. M1 revealed by quantitative proteomics. OMICS 2007, 11(3):233-251.
    • (2007) OMICS , vol.11 , Issue.3 , pp. 233-251
    • Santos, P.M.1    Roma, V.2    Benndorf, D.3    von Bergen, M.4    Harm, H.5    Sá-Correia, I.6
  • 170
    • 60549092710 scopus 로고    scopus 로고
    • Insights into yeast adaptive response to the agricultural fungicide mancozeb: a toxicoproteomics approach
    • Santos P.M., Simões T., Sá-Correia I. Insights into yeast adaptive response to the agricultural fungicide mancozeb: a toxicoproteomics approach. Proteomics 2009, 9(3):657-670.
    • (2009) Proteomics , vol.9 , Issue.3 , pp. 657-670
    • Santos, P.M.1    Simões, T.2    Sá-Correia, I.3
  • 171
    • 0342758523 scopus 로고    scopus 로고
    • Phosphite oxidation by sulphate reduction
    • Schink B., Friedrich M. Phosphite oxidation by sulphate reduction. Nature 2000, 406(6791):37.
    • (2000) Nature , vol.406 , Issue.6791 , pp. 37
    • Schink, B.1    Friedrich, M.2
  • 172
    • 1842499791 scopus 로고    scopus 로고
    • Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry
    • Schirle M., Heurtier M.A., Kuster B. Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry. Mol. Cell. Proteomics 2003, 2(12):1297-1305.
    • (2003) Mol. Cell. Proteomics , vol.2 , Issue.12 , pp. 1297-1305
    • Schirle, M.1    Heurtier, M.A.2    Kuster, B.3
  • 173
    • 2542574741 scopus 로고    scopus 로고
    • Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology
    • Schmidt F., Donahoe S., Hagens K., Mattow J., Schaible U.E., Kaufmann S.H., Aebersold R., Jungblut P.R. Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology. Mol. Cell. Proteomics 2004, 3(1):24-42.
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.1 , pp. 24-42
    • Schmidt, F.1    Donahoe, S.2    Hagens, K.3    Mattow, J.4    Schaible, U.E.5    Kaufmann, S.H.6    Aebersold, R.7    Jungblut, P.R.8
  • 174
    • 48949083987 scopus 로고    scopus 로고
    • Comparative proteomic and transcriptional profiling of a bread wheat cultivar and its derived transgenic line overexpressing a low molecular weight glutenin subunit gene in the endosperm
    • Scossa F., Laudencia-Chingcuanco D., Anderson O.D., Vensel W.H., Lafiandra D., D'Ovidio R., Masci S. Comparative proteomic and transcriptional profiling of a bread wheat cultivar and its derived transgenic line overexpressing a low molecular weight glutenin subunit gene in the endosperm. Proteomics 2008, 8(14):2948-2966.
    • (2008) Proteomics , vol.8 , Issue.14 , pp. 2948-2966
    • Scossa, F.1    Laudencia-Chingcuanco, D.2    Anderson, O.D.3    Vensel, W.H.4    Lafiandra, D.5    D'Ovidio, R.6    Masci, S.7
  • 175
    • 24344489015 scopus 로고    scopus 로고
    • Proteomic analysis reveals the participation of energy- and stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene
    • Segura A., Godoy P., van Dillewijn P., Hurtado A., Arroyo N., Santacruz S., Ramos J.L. Proteomic analysis reveals the participation of energy- and stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene. J. Bacteriol. 2005, 187:5937-5945.
    • (2005) J. Bacteriol. , vol.187 , pp. 5937-5945
    • Segura, A.1    Godoy, P.2    van Dillewijn, P.3    Hurtado, A.4    Arroyo, N.5    Santacruz, S.6    Ramos, J.L.7
  • 178
    • 19944426081 scopus 로고    scopus 로고
    • Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides ethenogenes.
    • Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A., et al. Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides ethenogenes. Science 2005, 307:105-108.
    • (2005) Science , vol.307 , pp. 105-108
    • Seshadri, R.1    Adrian, L.2    Fouts, D.E.3    Eisen, J.A.4    Phillippy, A.M.5    Methe, B.A.6
  • 179
    • 27744497057 scopus 로고    scopus 로고
    • Protein and peptide identification algorithms using MS for use in high-throughput, automated pipelines
    • Shadforth I., Crowther D., Bessant C. Protein and peptide identification algorithms using MS for use in high-throughput, automated pipelines. Proteomics 2005, 5(16):4082-4095.
    • (2005) Proteomics , vol.5 , Issue.16 , pp. 4082-4095
    • Shadforth, I.1    Crowther, D.2    Bessant, C.3
  • 180
    • 33750127867 scopus 로고    scopus 로고
    • GAPP: a fully automated software for the confident identification of human peptides from tandem mass spectra
    • Shadforth I., Xu W., Crowther D., Bessant C. GAPP: a fully automated software for the confident identification of human peptides from tandem mass spectra. J. Proteome Res. 2006, 5(10):2849-2852.
    • (2006) J. Proteome Res. , vol.5 , Issue.10 , pp. 2849-2852
    • Shadforth, I.1    Xu, W.2    Crowther, D.3    Bessant, C.4
  • 182
    • 16544366784 scopus 로고    scopus 로고
    • 13C-labeling experiments and integration of the information with gene and protein expression patterns
    • 13C-labeling experiments and integration of the information with gene and protein expression patterns. Adv. Biochem. Eng. Biotechnol. 2004, 91:1-49.
    • (2004) Adv. Biochem. Eng. Biotechnol. , vol.91 , pp. 1-49
    • Shimizu, K.1
  • 183
    • 51449111327 scopus 로고    scopus 로고
    • Structural proteomics by NMR spectroscopy
    • Shin J., Lee W., Lee W. Structural proteomics by NMR spectroscopy. Expert Rev. Proteomics 2008, 5(4):589-601.
    • (2008) Expert Rev. Proteomics , vol.5 , Issue.4 , pp. 589-601
    • Shin, J.1    Lee, W.2    Lee, W.3
  • 184
    • 33750584707 scopus 로고    scopus 로고
    • Proteomics and metabolomics: The molecular make-up of toxic aromatic pollutant bioremediation
    • Singh O.V. Proteomics and metabolomics: The molecular make-up of toxic aromatic pollutant bioremediation. Proteomics 2006, 6:5481-5492.
    • (2006) Proteomics , vol.6 , pp. 5481-5492
    • Singh, O.V.1
  • 185
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • Siuti N., Kelleher N.L. Decoding protein modifications using top-down mass spectrometry. Nat. Methods 2007, 4(10):817-821.
    • (2007) Nat. Methods , vol.4 , Issue.10 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 186
    • 2942724347 scopus 로고    scopus 로고
    • Proteomic analysis of Arabidopsis glutathione S-transferases from benoxacor- and copper-treated seedlings
    • Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E., Goldsbrough P.B. Proteomic analysis of Arabidopsis glutathione S-transferases from benoxacor- and copper-treated seedlings. J. Biol. Chem. 2004, 279(25):26098-26104.
    • (2004) J. Biol. Chem. , vol.279 , Issue.25 , pp. 26098-26104
    • Smith, A.P.1    DeRidder, B.P.2    Guo, W.J.3    Seeley, E.H.4    Regnier, F.E.5    Goldsbrough, P.B.6
  • 187
  • 188
    • 4143137559 scopus 로고    scopus 로고
    • Novel organization of genes in a phthalate degradation operon of Mycobacterium vanbaalenii PYR-1
    • Stingley R.L., Brezna B., Khan A.A., Cerniglia C.E. Novel organization of genes in a phthalate degradation operon of Mycobacterium vanbaalenii PYR-1. Microbiology 2004, 150(11):3749-3761.
    • (2004) Microbiology , vol.150 , Issue.11 , pp. 3749-3761
    • Stingley, R.L.1    Brezna, B.2    Khan, A.A.3    Cerniglia, C.E.4
  • 189
    • 0004268763 scopus 로고    scopus 로고
    • AMS Press, Washington, DC, G. Storz, R. Hengge-Aronis (Eds.)
    • Bacterial Stress Responses 2000, AMS Press, Washington, DC. G. Storz, R. Hengge-Aronis (Eds.).
    • (2000) Bacterial Stress Responses
  • 192
    • 0037953090 scopus 로고    scopus 로고
    • Similarity among tandem mass spectra from proteomic experiments: Detection, significance, and utility
    • Tabb D.L., MacCoss M.J., Wu C.C., Anderson S.D., Yates J.R. Similarity among tandem mass spectra from proteomic experiments: Detection, significance, and utility. Anal. Chem. 2003, 75(10):2470-2477.
    • (2003) Anal. Chem. , vol.75 , Issue.10 , pp. 2470-2477
    • Tabb, D.L.1    MacCoss, M.J.2    Wu, C.C.3    Anderson, S.D.4    Yates, J.R.5
  • 193
    • 27544511899 scopus 로고    scopus 로고
    • InsPecT: identification of posttranslationally modified peptides from tandem mass spectra
    • Tanner S., Shu H., Frank A., Wang L.C., Zandi E., Mumby M., Pevzner P.A., Bafna V. InsPecT: identification of posttranslationally modified peptides from tandem mass spectra. Anal. Chem. 2005, 77(14):4626-4639.
    • (2005) Anal. Chem. , vol.77 , Issue.14 , pp. 4626-4639
    • Tanner, S.1    Shu, H.2    Frank, A.3    Wang, L.C.4    Zandi, E.5    Mumby, M.6    Pevzner, P.A.7    Bafna, V.8
  • 194
    • 18844392542 scopus 로고    scopus 로고
    • A proteome analysis of the yeast response to the herbicide 2,4-dichlorophenoxyacetic acid
    • Teixeira M.C., Santos P.M., Fernandes A.R., Sá-Correia I. A proteome analysis of the yeast response to the herbicide 2,4-dichlorophenoxyacetic acid. Proteomics 2005, 5(7):1889-1901.
    • (2005) Proteomics , vol.5 , Issue.7 , pp. 1889-1901
    • Teixeira, M.C.1    Santos, P.M.2    Fernandes, A.R.3    Sá-Correia, I.4
  • 196
    • 33750591905 scopus 로고    scopus 로고
    • Proteomic and transcriptional characterization of aromatic degradation pathways in Rhodococcus sp. strain TFB
    • Tomàs-Gallardo L., Canosa I., Santero E., Camafeita E., Calvo E., López J.A., Floriano B. Proteomic and transcriptional characterization of aromatic degradation pathways in Rhodococcus sp. strain TFB. Proteomics 2006, 6(Suppl 1):S119-S132.
    • (2006) Proteomics , vol.6 , Issue.SUPPL.1
    • Tomàs-Gallardo, L.1    Canosa, I.2    Santero, E.3    Camafeita, E.4    Calvo, E.5    López, J.A.6    Floriano, B.7
  • 197
    • 2942750071 scopus 로고    scopus 로고
    • Mass spectrometric mapping of the enzymes involved in the phenol degradation of an indigenous soil pseudomonad
    • Tsirogianni E., Aivaliotis M., Karas M., Tsiotis G. Mass spectrometric mapping of the enzymes involved in the phenol degradation of an indigenous soil pseudomonad. Biochim. Biophys. Acta 2004, 1700(1):117-123.
    • (2004) Biochim. Biophys. Acta , vol.1700 , Issue.1 , pp. 117-123
    • Tsirogianni, E.1    Aivaliotis, M.2    Karas, M.3    Tsiotis, G.4
  • 198
    • 32944457963 scopus 로고    scopus 로고
    • Identification of inducible protein complexes in the phenol degrader Pseudomonas sp. strain phDV1 by blue native gel electrophoresis and mass spectrometry
    • Tsirogianni E., Aivaliotis M., Papasotiriou D.G., Karas M., Tsiotis G. Identification of inducible protein complexes in the phenol degrader Pseudomonas sp. strain phDV1 by blue native gel electrophoresis and mass spectrometry. Amino Acids 2006, 30(1):63-72.
    • (2006) Amino Acids , vol.30 , Issue.1 , pp. 63-72
    • Tsirogianni, E.1    Aivaliotis, M.2    Papasotiriou, D.G.3    Karas, M.4    Tsiotis, G.5
  • 199
    • 0032899676 scopus 로고    scopus 로고
    • Induction and enhancement of stress proteins in a trichloroethylene degrading methanotrophic bacterium, Methylocystis sp. M
    • Uchiyama H., Shinohara Y., Tomioka N., Kusaskabe I. Induction and enhancement of stress proteins in a trichloroethylene degrading methanotrophic bacterium, Methylocystis sp. M. FEMS Microbiol. Lett. 1999, 170:125-130.
    • (1999) FEMS Microbiol. Lett. , vol.170 , pp. 125-130
    • Uchiyama, H.1    Shinohara, Y.2    Tomioka, N.3    Kusaskabe, I.4
  • 200
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis, a single gel method for detecting changes in protein extracts
    • Unlü M., Morgan M.E., Minden J.S. Difference gel electrophoresis, a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18(11):2071-2077.
    • (1997) Electrophoresis , vol.18 , Issue.11 , pp. 2071-2077
    • Unlü, M.1    Morgan, M.E.2    Minden, J.S.3
  • 201
    • 1242328741 scopus 로고    scopus 로고
    • Fluorescent two-dimensional difference gel electrophoresis unveils the potential of gel-based proteomics
    • van den Bergh G., Arckens L. Fluorescent two-dimensional difference gel electrophoresis unveils the potential of gel-based proteomics. Curr. Opin. Biotechnol. 2004, 15(1):38-43.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , Issue.1 , pp. 38-43
    • van den Bergh, G.1    Arckens, L.2
  • 203
    • 32344441400 scopus 로고    scopus 로고
    • Determination and comparison of the baseline proteomes of the versatile microbe Rhodopseudomonas palustris under its major metabolic states
    • VerBerkmoes N.C., Shah M.B., Lankford P.K., Pelletier D.A., Strader M.B., Tabb D.L., et al. Determination and comparison of the baseline proteomes of the versatile microbe Rhodopseudomonas palustris under its major metabolic states. J. Proteome Res. 2006, 5(2):287-298.
    • (2006) J. Proteome Res. , vol.5 , Issue.2 , pp. 287-298
    • VerBerkmoes, N.C.1    Shah, M.B.2    Lankford, P.K.3    Pelletier, D.A.4    Strader, M.B.5    Tabb, D.L.6
  • 205
    • 0003706002 scopus 로고    scopus 로고
    • Humana Press, Totowa, NJ, J.M. Walker (Ed.)
    • The Protein Protocols Handbook 2002, Humana Press, Totowa, NJ. 2nd ed. J.M. Walker (Ed.).
    • (2002) The Protein Protocols Handbook
  • 206
    • 0033770904 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of the katG gene, encoding catalase-peroxidase, from the polycyclic aromatic hydrocarbon-degrading bacterium Mycobacterium sp. strain PYR-1
    • Wang R.F., Wennerstrom D., Cao W.W., Khan A.A., Cerniglia C.E. Cloning, expression, and characterization of the katG gene, encoding catalase-peroxidase, from the polycyclic aromatic hydrocarbon-degrading bacterium Mycobacterium sp. strain PYR-1. Appl. Environ. Microbiol. 2000, 66(10):4300-4304.
    • (2000) Appl. Environ. Microbiol. , vol.66 , Issue.10 , pp. 4300-4304
    • Wang, R.F.1    Wennerstrom, D.2    Cao, W.W.3    Khan, A.A.4    Cerniglia, C.E.5
  • 207
    • 0028924094 scopus 로고
    • Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1
    • Wang Y., Rawlings M., Gibson D.T., Labbé D., Bergeron H., Brousseau R., Lau P.C. Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1. Mol. Gen. Genet. 1995, 246(5):570-579.
    • (1995) Mol. Gen. Genet. , vol.246 , Issue.5 , pp. 570-579
    • Wang, Y.1    Rawlings, M.2    Gibson, D.T.3    Labbé, D.4    Bergeron, H.5    Brousseau, R.6    Lau, P.C.7
  • 208
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19(3):242-247.
    • (2001) Nat. Biotechnol. , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 209
    • 0029033175 scopus 로고
    • Progress with gene-product mapping of the Mollicutes, Mycoplasma genitalium
    • Wasinger V.C. Progress with gene-product mapping of the Mollicutes, Mycoplasma genitalium. Electrophoresis 1995, 16(7):1090-1094.
    • (1995) Electrophoresis , vol.16 , Issue.7 , pp. 1090-1094
    • Wasinger, V.C.1
  • 210
    • 38549162759 scopus 로고    scopus 로고
    • CEBS"Chemical Effects in Biological Systems: a public data repository integrating study design and toxicity data with microarray and proteomics data
    • Database Issue
    • Waters M., Stasiewicz S., Merrick B.A., Tomer K., Bushel P., Paules R., et al. CEBS"Chemical Effects in Biological Systems: a public data repository integrating study design and toxicity data with microarray and proteomics data. Nucleic Acids Res. 2008, 36(database issue):D892-D900.
    • (2008) Nucleic Acids Res. , vol.36
    • Waters, M.1    Stasiewicz, S.2    Merrick, B.A.3    Tomer, K.4    Bushel, P.5    Paules, R.6
  • 212
    • 0035095051 scopus 로고    scopus 로고
    • Proteomics"The protein expression technology to study connective tissue biology
    • Westergren-Thorsson G., Malmström J., Marko-Varga G. Proteomics"The protein expression technology to study connective tissue biology. J. Pharm. Biomed. Anal. 2001, 24(5-6):815-824.
    • (2001) J. Pharm. Biomed. Anal. , vol.24 , Issue.5-6 , pp. 815-824
    • Westergren-Thorsson, G.1    Malmström, J.2    Marko-Varga, G.3
  • 215
    • 49449100328 scopus 로고    scopus 로고
    • Anaerobic degradation of p-ethylphenol by "Aromatoleum aromaticum" strain EbN1: pathway, regulation, and involved proteins
    • Wöhlbrand L., Wilkes H., Halder T., Rabus R. Anaerobic degradation of p-ethylphenol by "Aromatoleum aromaticum" strain EbN1: pathway, regulation, and involved proteins. J. Bacteriol. 2008, 190(16):5699-5709.
    • (2008) J. Bacteriol. , vol.190 , Issue.16 , pp. 5699-5709
    • Wöhlbrand, L.1    Wilkes, H.2    Halder, T.3    Rabus, R.4
  • 216
    • 36049014914 scopus 로고    scopus 로고
    • A comparison of nLC-ESI-MS-MS and nLC-MALDI-MS-MS for GeLC-based protein identification and iTRAQ-based shotgun quantitative proteomics
    • Yang Y., Zhang S., Howe K., Wilson D.B., Moser F., Irwin D., Thannhauser T.W. A comparison of nLC-ESI-MS-MS and nLC-MALDI-MS-MS for GeLC-based protein identification and iTRAQ-based shotgun quantitative proteomics. J. Biomol. Tech. 2007, 18(4):226-237.
    • (2007) J. Biomol. Tech. , vol.18 , Issue.4 , pp. 226-237
    • Yang, Y.1    Zhang, S.2    Howe, K.3    Wilson, D.B.4    Moser, F.5    Irwin, D.6    Thannhauser, T.W.7
  • 217
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates J., Ruse C.I., Nakorchevsky A. Proteomics by mass spectrometry: Approaches, advances, and applications. Annu. Rev. Biomed. Eng. 2009, 11:49-79.
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates, J.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 218
    • 34447282630 scopus 로고    scopus 로고
    • Characterization of a new catechol branch of the bη-ketoadipate pathway induced for benzoate degradation in Acinetobacter lwoffii K24
    • Yoon Y.H., Yun S.H., Park S.H., Seol S.Y., Leem S.H., Kim S.I. Characterization of a new catechol branch of the bη-ketoadipate pathway induced for benzoate degradation in Acinetobacter lwoffii K24. Biochem. Biophys. Res. Commun. 2007, 360:513-519.
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 513-519
    • Yoon, Y.H.1    Yun, S.H.2    Park, S.H.3    Seol, S.Y.4    Leem, S.H.5    Kim, S.I.6
  • 219
    • 33746762234 scopus 로고    scopus 로고
    • Proteome analysis of cellular response of Pseudomonas putida KT2440 to tetracycline stress
    • Yun S.H., Kim Y.H., Joo E.J., Choi J.S., Sohn J.H., Kim S.I. Proteome analysis of cellular response of Pseudomonas putida KT2440 to tetracycline stress. Curr. Microbiol. 2006, 53(2):95-101.
    • (2006) Curr. Microbiol. , vol.53 , Issue.2 , pp. 95-101
    • Yun, S.H.1    Kim, Y.H.2    Joo, E.J.3    Choi, J.S.4    Sohn, J.H.5    Kim, S.I.6
  • 220
    • 58149109275 scopus 로고    scopus 로고
    • Proteomic analysis of outer membrane proteins from Acinetobacter baumannii DU202 in tetracycline stress condition
    • Yun S.H., Choi C.W., Park S.H., Lee J.C., Leem S.H., Choi J.S., Kim S., Kim S.I. Proteomic analysis of outer membrane proteins from Acinetobacter baumannii DU202 in tetracycline stress condition. J. Microbiol. 2008, 46(6):720-727.
    • (2008) J. Microbiol. , vol.46 , Issue.6 , pp. 720-727
    • Yun, S.H.1    Choi, C.W.2    Park, S.H.3    Lee, J.C.4    Leem, S.H.5    Choi, J.S.6    Kim, S.7    Kim, S.I.8
  • 221
    • 3042818014 scopus 로고    scopus 로고
    • Proteomic characterization of herbicide safener-induced proteins in the coleoptile of Triticum tauschii seedlings
    • Zhang Q., Riechers D.E. Proteomic characterization of herbicide safener-induced proteins in the coleoptile of Triticum tauschii seedlings. Proteomics 2004, 4(7):2058-2071.
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 2058-2071
    • Zhang, Q.1    Riechers, D.E.2
  • 222
    • 34248137521 scopus 로고    scopus 로고
    • Safeners coordinately induce the expression of multiple proteins and MRP transcripts involved in herbicide metabolism and detoxification in Triticum tauschii seedling tissues
    • Zhang Q., Xu F., Lambert K.N., Riechers D.E. Safeners coordinately induce the expression of multiple proteins and MRP transcripts involved in herbicide metabolism and detoxification in Triticum tauschii seedling tissues. Proteomics 2007, 7(8):1261-1278.
    • (2007) Proteomics , vol.7 , Issue.8 , pp. 1261-1278
    • Zhang, Q.1    Xu, F.2    Lambert, K.N.3    Riechers, D.E.4
  • 223
    • 58149177511 scopus 로고    scopus 로고
    • Proteomic and molecular investigation on the physiological adaptation of Comamonas sp. strain CNB-1 growing on 4-chloronitrobenzene
    • Zhang Y., Wu J.F., Zeyer J., Meng B., Liu L., Jiang C.Y., Liu S.Q., Liu S.J. Proteomic and molecular investigation on the physiological adaptation of Comamonas sp. strain CNB-1 growing on 4-chloronitrobenzene. Biodegradation 2009, 20:55-66.
    • (2009) Biodegradation , vol.20 , pp. 55-66
    • Zhang, Y.1    Wu, J.F.2    Zeyer, J.3    Meng, B.4    Liu, L.5    Jiang, C.Y.6    Liu, S.Q.7    Liu, S.J.8
  • 224
    • 3042772559 scopus 로고    scopus 로고
    • Proteome analysis of gentisate-induced response in Pseudomonas alcaligenes NCIB 9867
    • Zhao B., Yeo C.C., Lee C.C., Geng A., Chew F.T., Poh C.L. Proteome analysis of gentisate-induced response in Pseudomonas alcaligenes NCIB 9867. Proteomics 2004, 4(7):2028-2036.
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 2028-2036
    • Zhao, B.1    Yeo, C.C.2    Lee, C.C.3    Geng, A.4    Chew, F.T.5    Poh, C.L.6
  • 225
    • 18844410520 scopus 로고    scopus 로고
    • Proteome investigation of the global regulatory role of sigma 54 in response to gentisate induction in Pseudomonas alcaligenes NCIMB 9867
    • Zhao B., Yeo C.C., Poh C.L. Proteome investigation of the global regulatory role of sigma 54 in response to gentisate induction in Pseudomonas alcaligenes NCIMB 9867. Proteomics 2005, 5:1868-1876.
    • (2005) Proteomics , vol.5 , pp. 1868-1876
    • Zhao, B.1    Yeo, C.C.2    Poh, C.L.3
  • 226
    • 34249802595 scopus 로고    scopus 로고
    • Proteome analysis of heat shock protein expression in Pseudomonas alcaligenes NCIMB 9867 in response to gentisate exposure and elevated growth temperature
    • Zhao B., Yeo C.C., Tan C.L., Poh C.L. Proteome analysis of heat shock protein expression in Pseudomonas alcaligenes NCIMB 9867 in response to gentisate exposure and elevated growth temperature. Biotechnol. Bioeng. 2007, 97(3):506-514.
    • (2007) Biotechnol. Bioeng. , vol.97 , Issue.3 , pp. 506-514
    • Zhao, B.1    Yeo, C.C.2    Tan, C.L.3    Poh, C.L.4
  • 227
    • 52049102730 scopus 로고    scopus 로고
    • Proteomics as a complementary tool for identifying unintended side effects occurring in transgenic maize seeds as a result of genetic modifications
    • Zolla L., Rinalducci S., Antonioli P., Righetti P.G. Proteomics as a complementary tool for identifying unintended side effects occurring in transgenic maize seeds as a result of genetic modifications. J. Proteome Res. 2008, 7(5):1850-1861.
    • (2008) J. Proteome Res. , vol.7 , Issue.5 , pp. 1850-1861
    • Zolla, L.1    Rinalducci, S.2    Antonioli, P.3    Righetti, P.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.