메뉴 건너뛰기




Volumn 11, Issue 1-2, 2006, Pages 53-81

Mass spectrometric identification of proteins in complex post-genomic projects: Soluble proteins of the metabolically versatile, denitrifying 'Aromatoleum' sp. strain EbN1

Author keywords

2D DIGE; Anaerobic degradation; Aromatic compounds; Bioinformatics; High throughput; Ion trap; LC ESI; MALDI TOF; Mass spectrometry; MS MS; Protein identification; Proteomics; Quantitative proteomics; Robotics; Two dimensional gel electrophoresis

Indexed keywords

ALGORITHM; AROMATOLEUM; ARTICLE; AUTOMATION; BACTERIAL GENOME; BACTERIAL STRAIN; BACTERIUM; BIOINFORMATICS; CALIBRATION; DENITRIFICATION; GENOME ANALYSIS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PROTEIN ANALYSIS; PROTEOMICS; REPRODUCIBILITY; TANDEM MASS SPECTROMETRY; TWO DIMENSIONAL GEL ELECTROPHORESIS;

EID: 33745742167     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: 10.1159/000092819     Document Type: Article
Times cited : (25)

References (201)
  • 1
  • 3
    • 0347755458 scopus 로고    scopus 로고
    • GELBANK: A database of annotated two-dimensional gel electrophoresis patterns of biological systems with completed genomes
    • Babnigg G, Giometti CS (2004) GELBANK: a database of annotated two-dimensional gel electrophoresis patterns of biological systems with completed genomes. Nucleic Acids Res 32:D582-D585.
    • (2004) Nucleic Acids Res , vol.32
    • Babnigg, G.1    Giometti, C.S.2
  • 4
    • 17044389822 scopus 로고    scopus 로고
    • Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry
    • Backert S, Kwok T, Schmid M, Selbach M, Moese S, Peek Jr RM, König W, Meyer TF, Jungblut PR (2005) Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry. Proteomics 5:1331-1345.
    • (2005) Proteomics , vol.5 , pp. 1331-1345
    • Backert, S.1    Kwok, T.2    Schmid, M.3    Selbach, M.4    Moese, S.5    Peek Jr., R.M.6    König, W.7    Meyer, T.F.8    Jungblut, P.R.9
  • 5
    • 0002451984 scopus 로고    scopus 로고
    • SCOPE: A probabilistic model for scoring tandem mass spectra against a peptide database
    • Bafna V, Edwards N (2001) SCOPE: a probabilistic model for scoring tandem mass spectra against a peptide database. Bioinformatics 17:S13-S21.
    • (2001) Bioinformatics , vol.17
    • Bafna, V.1    Edwards, N.2
  • 7
    • 0023399896 scopus 로고
    • Characterization by tandem mass spectrometry of structural modifications in proteins
    • Biemann K, Scoble HA (1987) Characterization by tandem mass spectrometry of structural modifications in proteins. Science 237:992-998.
    • (1987) Science , vol.237 , pp. 992-998
    • Biemann, K.1    Scoble, H.A.2
  • 8
    • 0003128903 scopus 로고    scopus 로고
    • Electrospray-ionization quadrupole ion-trap mass spectrometry
    • Cole RB (ed): John Wiley & Sons Inc., New York
    • Bier ME, Schwartz JC (1997) Electrospray-ionization quadrupole ion-trap mass spectrometry; in Cole RB (ed): Electrospray Ionization Mass Spectrometry. John Wiley & Sons Inc., New York, pp 235-288.
    • (1997) Electrospray Ionization Mass Spectrometry , pp. 235-288
    • Bier, M.E.1    Schwartz, J.C.2
  • 11
    • 14744304574 scopus 로고    scopus 로고
    • Proteomics by FTI-CR mass spectrometry: Top down and bottom up
    • Bogdanov B, Smith RD (2005) Proteomics by FTI-CR mass spectrometry: top down and bottom up. Mass Spectrom Rev 24:168-200.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 168-200
    • Bogdanov, B.1    Smith, R.D.2
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 84984932472 scopus 로고    scopus 로고
    • Exploring the new world of the genome with DNA microarrays
    • Brown PO, Botstein D (1999) Exploring the new world of the genome with DNA microarrays. Nat Gen 21:33-37.
    • (1999) Nat Gen , vol.21 , pp. 33-37
    • Brown, P.O.1    Botstein, D.2
  • 18
    • 1542720811 scopus 로고    scopus 로고
    • Evaluation of algorithms for protein identification from sequence databases using mass spectrometry data
    • Chamrad DC, Körting G, Stühler K, Meyer HE, Klose J, Blüggel M (2004) Evaluation of algorithms for protein identification from sequence databases using mass spectrometry data. Proteomics 4:619-628.
    • (2004) Proteomics , vol.4 , pp. 619-628
    • Chamrad, D.C.1    Körting, G.2    Stühler, K.3    Meyer, H.E.4    Klose, J.5    Blüggel, M.6
  • 19
  • 20
    • 0034852208 scopus 로고    scopus 로고
    • An introduction to quadrupole-time-of-flight mass spectrometry
    • Chernushevich IV, Loboda AV, Thomson BA (2001) An introduction to quadrupole-time-of-flight mass spectrometry. J Mass Spectrom 36:849-865.
    • (2001) J Mass Spectrom , vol.36 , pp. 849-865
    • Chernushevich, I.V.1    Loboda, A.V.2    Thomson, B.A.3
  • 21
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser KR, Baker P, Burlingame AL (1999) Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal Chem 71:2871-2882.
    • (1999) Anal Chem , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 23
    • 12244270638 scopus 로고    scopus 로고
    • Differential proteomics via probabilistic peptide identification scores
    • Colinge J, Chiappe D, Lagache S, Moniatte M, Bougueleret L (2005) Differential proteomics via probabilistic peptide identification scores. Anal Chem 77:596-606.
    • (2005) Anal Chem , vol.77 , pp. 596-606
    • Colinge, J.1    Chiappe, D.2    Lagache, S.3    Moniatte, M.4    Bougueleret, L.5
  • 24
    • 0037323796 scopus 로고    scopus 로고
    • Microarray expression profiling: Capturing a genome-wide portrait of the transcriptome
    • Conway T, Schoolnik GK (2003) Microarray expression profiling: capturing a genome-wide portrait of the transcriptome. Mol Microbiol 47:879-889.
    • (2003) Mol Microbiol , vol.47 , pp. 879-889
    • Conway, T.1    Schoolnik, G.K.2
  • 25
    • 0034013175 scopus 로고    scopus 로고
    • Subproteomics based upon protein cellular location and relative solubilities in conjunction with composite two-dimensional electrophoresis
    • Cordwell SJ, Nouwens AS, Verrills NM, Basseal DJ, Walsh BJ (2000) Subproteomics based upon protein cellular location and relative solubilities in conjunction with composite two-dimensional electrophoresis. Electrophoresis 21:1094-1103.
    • (2000) Electrophoresis , vol.21 , pp. 1094-1103
    • Cordwell, S.J.1    Nouwens, A.S.2    Verrills, N.M.3    Basseal, D.J.4    Walsh, B.J.5
  • 27
    • 20544468239 scopus 로고    scopus 로고
    • High-throughput proteomics using matrix-assisted laser desorption/ionization mass spectrometry
    • Cramer R, Gobom J, Nordhoff E (2005) High-throughput proteomics using matrix-assisted laser desorption/ionization mass spectrometry. Expert Rev Proteomics 2:407-420.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 407-420
    • Cramer, R.1    Gobom, J.2    Nordhoff, E.3
  • 29
    • 3042772563 scopus 로고    scopus 로고
    • Sinorhizobium meliloti metabolism in the root nodule: A proteomic perspective
    • Djordjevic MA (2004) Sinorhizobium meliloti metabolism in the root nodule: a proteomic perspective. Proteomics 4:1859-1872.
    • (2004) Proteomics , vol.4 , pp. 1859-1872
    • Djordjevic, M.A.1
  • 30
    • 0031887006 scopus 로고    scopus 로고
    • Analysis of changes in acute-phase plasma proteins in an acute inflammatory response and in rheumatoid arthritis using two-dimensional gel electrophoresis
    • Doherty NS, Littman BH, Reilly K, Swindell AC, Buss JM, Anderson NL (1998) Analysis of changes in acute-phase plasma proteins in an acute inflammatory response and in rheumatoid arthritis using two-dimensional gel electrophoresis. Electrophoresis 19:355-363.
    • (1998) Electrophoresis , vol.19 , pp. 355-363
    • Doherty, N.S.1    Littman, B.H.2    Reilly, K.3    Swindell, A.C.4    Buss, J.M.5    Anderson, N.L.6
  • 31
    • 13444251413 scopus 로고    scopus 로고
    • DynaProt 2D: An advanced proteomic database for dynamic online access to proteomes and two-dimensional electrophoresis gels
    • Drews O, Görg A (2005) DynaProt 2D: an advanced proteomic database for dynamic online access to proteomes and two-dimensional electrophoresis gels. Nucleic Acids Res 33:D583-D587.
    • (2005) Nucleic Acids Res , vol.33
    • Drews, O.1    Görg, A.2
  • 32
    • 2442568591 scopus 로고    scopus 로고
    • Setting up standards and a reference map for the alkaline proteome of the Gram-positive bacterium Lactococcus lactis
    • Drews O, Reil G, Parlar H, Görg A (2004) Setting up standards and a reference map for the alkaline proteome of the Gram-positive bacterium Lactococcus lactis. Proteomics 4:1293-1304.
    • (2004) Proteomics , vol.4 , pp. 1293-1304
    • Drews, O.1    Reil, G.2    Parlar, H.3    Görg, A.4
  • 33
    • 28544436158 scopus 로고    scopus 로고
    • Classification and identification of bacteria using mass-spectrometry- based proteomics
    • Dworzanski JP, Snyder AP (2005) Classification and identification of bacteria using mass-spectrometry-based proteomics. Expert Rev Proteomics 2:863-878.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 863-878
    • Dworzanski, J.P.1    Snyder, A.P.2
  • 36
    • 23244467936 scopus 로고    scopus 로고
    • Proteome analysis of serovars Typhimurium and Pullorum of Salmonella enterica subspecies I
    • Encheva V, Wait R, Gharbia SE, Begum S, Shah HN (2005) Proteome analysis of serovars Typhimurium and Pullorum of Salmonella enterica subspecies I. BMC Microbiol 5:42.
    • (2005) BMC Microbiol , vol.5 , pp. 42
    • Encheva, V.1    Wait, R.2    Gharbia, S.E.3    Begum, S.4    Shah, H.N.5
  • 37
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates 3rd JR (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5:976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 39
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 40
    • 0033887451 scopus 로고    scopus 로고
    • Identifying the proteome: Software tools
    • Fenyö D (2000) Identifying the proteome: software tools. Curr Opin Biotechnol 11:391-395.
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 391-395
    • Fenyö, D.1
  • 41
    • 0031865293 scopus 로고    scopus 로고
    • Protein identification using mass spectrometric information
    • Fenyö D, Qin J, Chait BT (1998) Protein identification using mass spectrometric information. Electrophoresis 19:998-1005.
    • (1998) Electrophoresis , vol.19 , pp. 998-1005
    • Fenyö, D.1    Qin, J.2    Chait, B.T.3
  • 42
    • 0036211823 scopus 로고    scopus 로고
    • RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimizes protein identification, and archives data in a relational database
    • Field HI, Fenyö D, Beavis RC (2002) RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimizes protein identification, and archives data in a relational database. Proteomics 2:36-47.
    • (2002) Proteomics , vol.2 , pp. 36-47
    • Field, H.I.1    Fenyö, D.2    Beavis, R.C.3
  • 45
    • 5644220088 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis database of Listeria monocytogenes EGDe proteome and proteomic analysis of mid-log and stationary growth phase cells
    • Folio P, Chavant P, Chafsey I, Belkorchia A, Chambon C, Hébraud M (2004) Two-dimensional electrophoresis database of Listeria monocytogenes EGDe proteome and proteomic analysis of mid-log and stationary growth phase cells. Proteomics 4:3187-3201.
    • (2004) Proteomics , vol.4 , pp. 3187-3201
    • Folio, P.1    Chavant, P.2    Chafsey, I.3    Belkorchia, A.4    Chambon, C.5    Hébraud, M.6
  • 46
    • 27944473728 scopus 로고    scopus 로고
    • Response of the anaerobe Desulfovibrio vulgaris Hildenborough to oxidative conditions: Proteome and transcript analysis
    • Fournier M, Aubert C, Dermoun Z, Durand M-C, Moinier D, Dolla A (2005) Response of the anaerobe Desulfovibrio vulgaris Hildenborough to oxidative conditions: proteome and transcript analysis. Biochemie 88:85-94.
    • (2005) Biochemie , vol.88 , pp. 85-94
    • Fournier, M.1    Aubert, C.2    Dermoun, Z.3    Durand, M.-C.4    Moinier, D.5    Dolla, A.6
  • 47
    • 0002176847 scopus 로고
    • Nonlinear ion traps in practical aspects of ion trap mass spectrometry
    • March RE, Todd JFJ (eds): CRC Press, Boca Raton
    • Franzen J, Gabling R-H, Schubert M, Wang Y (1995) Nonlinear ion traps in practical aspects of ion trap mass spectrometry; in March RE, Todd JFJ (eds): Fundamentals of Ion Trap Mass Spectrometry, Volume I. CRC Press, Boca Raton, pp. 49-167.
    • (1995) Fundamentals of Ion Trap Mass Spectrometry , vol.1 , pp. 49-167
    • Franzen, J.1    Gabling, R.-H.2    Schubert, M.3    Wang, Y.4
  • 48
    • 0032526322 scopus 로고    scopus 로고
    • Combining diverse evidence for gene recognition in completely sequenced bacterial genomes
    • Frishman D, Mironov A, Mewes H-W, Gelfand M (1998) Combining diverse evidence for gene recognition in completely sequenced bacterial genomes. Nucleic Acids Res 26:2941-2947.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2941-2947
    • Frishman, D.1    Mironov, A.2    Mewes, H.-W.3    Gelfand, M.4
  • 49
    • 22744459517 scopus 로고    scopus 로고
    • Proteomic analysis of carbohydrate catabolism and regulation in the marine bacterium Rhodopirellula baltica
    • Gade D, Gobom J, Rabus R (2005a) Proteomic analysis of carbohydrate catabolism and regulation in the marine bacterium Rhodopirellula baltica. Proteomics 5:3672-3683.
    • (2005) Proteomics , vol.5 , pp. 3672-3683
    • Gade, D.1    Gobom, J.2    Rabus, R.3
  • 50
    • 22744436104 scopus 로고    scopus 로고
    • Growth phase dependent regulation of protein composition in Rhodopirellula baltica
    • Gade D, Stührmann T, Reinhardt R, Rabus R (2005b) Growth phase dependent regulation of protein composition in Rhodopirellula baltica. Environ Microbiol 7:1074-1084.
    • (2005) Environ Microbiol , vol.7 , pp. 1074-1084
    • Gade, D.1    Stührmann, T.2    Reinhardt, R.3    Rabus, R.4
  • 52
    • 0041871026 scopus 로고    scopus 로고
    • Evaluation of two-dimensional difference gel electrophoresis for protein profiling. Soluble proteins of the marine bacterium Pirellula sp. strain 1
    • Gade D, Thiermann J, Markowsky D, Rabus R (2003) Evaluation of two-dimensional difference gel electrophoresis for protein profiling. Soluble proteins of the marine bacterium Pirellula sp. strain 1. J Mol Microbiol Biotechnol 5:240-251.
    • (2003) J Mol Microbiol Biotechnol , vol.5 , pp. 240-251
    • Gade, D.1    Thiermann, J.2    Markowsky, D.3    Rabus, R.4
  • 53
    • 13444259868 scopus 로고    scopus 로고
    • The molecular biology database collection: 2005 Update
    • Galperin MY (2005) The molecular biology database collection: 2005 update. Nucleic Acids Res 33:D5-D24.
    • (2005) Nucleic Acids Res , vol.33
    • Galperin, M.Y.1
  • 59
    • 0035253337 scopus 로고    scopus 로고
    • α-Cyano-4-hydroxycinnamic acid affinity sample preparation. A protocol for MALDI-MS peptide analysis in proteomics
    • Gobom J, Schürenberg M, Müller M, Theiss D, Lehrach H, Nordhoff E (2001) α-Cyano-4-hydroxycinnamic acid affinity sample preparation. A protocol for MALDI-MS peptide analysis in proteomics. Anal Chem 73:434-438.
    • (2001) Anal Chem , vol.73 , pp. 434-438
    • Gobom, J.1    Schürenberg, M.2    Müller, M.3    Theiss, D.4    Lehrach, H.5    Nordhoff, E.6
  • 61
    • 10044245551 scopus 로고    scopus 로고
    • Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry
    • Goodchild A, Raftery M, Saunders NFW, Guilhaus M, Cavicchioli R (2004) Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry. J Proteome Res 3:1164-1176.
    • (2004) J Proteome Res , vol.3 , pp. 1164-1176
    • Goodchild, A.1    Raftery, M.2    Saunders, N.F.W.3    Guilhaus, M.4    Cavicchioli, R.5
  • 62
    • 0036917339 scopus 로고    scopus 로고
    • Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels
    • Görg A, Boguth G, Köpf A, Reil G, Parlar H, Weiss W (2002) Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels. Proteomics 2:1652-1657.
    • (2002) Proteomics , vol.2 , pp. 1652-1657
    • Görg, A.1    Boguth, G.2    Köpf, A.3    Reil, G.4    Parlar, H.5    Weiss, W.6
  • 64
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Görg A, Weiss W, Dunn MJ (2004) Current two-dimensional electrophoresis technology for proteomics. Proteomics 4:3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Görg, A.1    Weiss, W.2    Dunn, M.J.3
  • 65
    • 14844293459 scopus 로고    scopus 로고
    • Broad-based proteomic strategies: A practical guide to proteomics and functional screening
    • Graham DRM, Elliott ST, Van Eyk JE (2005) Broad-based proteomic strategies: a practical guide to proteomics and functional screening. J Physiol 563:1-9.
    • (2005) J Physiol , vol.563 , pp. 1-9
    • Graham, D.R.M.1    Elliott, S.T.2    Van Eyk, J.E.3
  • 68
  • 69
    • 0037398266 scopus 로고    scopus 로고
    • Interfacing the Orbitrap mass analyzer to an electrospray ion source
    • Hardman M, Makarov AA (2003) Interfacing the Orbitrap mass analyzer to an electrospray ion source. Anal Chem 75:1699-1705.
    • (2003) Anal Chem , vol.75 , pp. 1699-1705
    • Hardman, M.1    Makarov, A.A.2
  • 70
    • 0038782226 scopus 로고    scopus 로고
    • Gene expression analysis of energy metabolism mutants of Desulfovibrio vulgaris Hildenborough indicates an important role of alcohol dehydrogenase
    • Haveman SA, Brunelle V, Voordouw JK, Voordouw G, Heidelberg JF, Rabus R (2003) Gene expression analysis of energy metabolism mutants of Desulfovibrio vulgaris Hildenborough indicates an important role of alcohol dehydrogenase. J Bacteriol 185:4345-4353.
    • (2003) J Bacteriol , vol.185 , pp. 4345-4353
    • Haveman, S.A.1    Brunelle, V.2    Voordouw, J.K.3    Voordouw, G.4    Heidelberg, J.F.5    Rabus, R.6
  • 71
    • 0037420419 scopus 로고    scopus 로고
    • Proteomics of Staphylococcus aureus - Current state and future challenges
    • Hecker M, Engelmann S, Cordwell SJ (2003) Proteomics of Staphylococcus aureus - current state and future challenges. J Chromatogr B 787:179-195.
    • (2003) J Chromatogr B , vol.787 , pp. 179-195
    • Hecker, M.1    Engelmann, S.2    Cordwell, S.J.3
  • 72
    • 10644274361 scopus 로고    scopus 로고
    • Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics
    • Hecker M, Völker U (2004) Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics. Proteomics 4:3727-3750.
    • (2004) Proteomics , vol.4 , pp. 3727-3750
    • Hecker, M.1    Völker, U.2
  • 73
    • 0031018959 scopus 로고    scopus 로고
    • Anaerobic metabolism of aromatic compounds
    • Heider J, Fuchs G (1997) Anaerobic metabolism of aromatic compounds. Eur J Biochem 243:577-596.
    • (1997) Eur J Biochem , vol.243 , pp. 577-596
    • Heider, J.1    Fuchs, G.2
  • 74
    • 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 KN (2003) 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 5:1257-1269.
    • (2003) Environ Microbiol , vol.5 , pp. 1257-1269
    • Heim, S.1    Ferrer, M.2    Heuer, H.3    Regenhardt, D.4    Nimtz, M.5    Timmis, K.N.6
  • 75
    • 0036433469 scopus 로고    scopus 로고
    • Primary and secondary metabolism, and post-translational protein modifications, as portrayed by proteomic analysis of Streptomyces coelicolor
    • Hesketh AR, Chandra G, Shaw AD, Rowland JJ, Kell DB, Bibb MJ, Chater KF (2002) Primary and secondary metabolism, and post-translational protein modifications, as portrayed by proteomic analysis of Streptomyces coelicolor. Mol Microbiol 46:917-932.
    • (2002) Mol Microbiol , vol.46 , pp. 917-932
    • Hesketh, A.R.1    Chandra, G.2    Shaw, A.D.3    Rowland, J.J.4    Kell, D.B.5    Bibb, M.J.6    Chater, K.F.7
  • 76
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in Phast-System Development Unit. I. Staining of sodium dodecyl sulfate gels
    • Heukeshoven J, Dernick R (1988) Improved silver staining procedure for fast staining in Phast-System Development Unit. I. Staining of sodium dodecyl sulfate gels. Electrophoresis 9:28-32.
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 79
    • 0028879976 scopus 로고
    • Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins
    • Houthaeve T, Gausepohl H, Mann M, Ashman K (1995) Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins. FEBS Lett 376:91-94.
    • (1995) FEBS Lett , vol.376 , pp. 91-94
    • Houthaeve, T.1    Gausepohl, H.2    Mann, M.3    Ashman, K.4
  • 84
    • 17044435511 scopus 로고    scopus 로고
    • Proteomic analysis of Lyme disease: Global protein comparison of three strains of Borrelia burgdorferi
    • Jacobs JM, Yang X, Luft BJ, Dunn JJ, Camp II DG, Smith RD (2005) Proteomic analysis of Lyme disease: global protein comparison of three strains of Borrelia burgdorferi. Proteomics 5:1446-1453.
    • (2005) Proteomics , vol.5 , pp. 1446-1453
    • Jacobs, J.M.1    Yang, X.2    Luft, B.J.3    Dunn, J.J.4    Camp II, D.G.5    Smith, R.D.6
  • 86
    • 0023449998 scopus 로고
    • Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: Differentiation of leucine and isoleucine
    • Johnson RS, Martin SA, Biemann K, Stults JT, Watson JT (1987) Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: differentiation of leucine and isoleucine. Anal Chem 59:2621-2625.
    • (1987) Anal Chem , vol.59 , pp. 2621-2625
    • Johnson, R.S.1    Martin, S.A.2    Biemann, K.3    Stults, J.T.4    Watson, J.T.5
  • 88
    • 4544249264 scopus 로고    scopus 로고
    • Protein profile of symbiotic bacteria Mesorhizobium loti MAFF303099 in mid-growth phase
    • Kajiwara H, Kaneko T, Ishizaka M, Tajima S, Kouchi H (2003) Protein profile of symbiotic bacteria Mesorhizobium loti MAFF303099 in mid-growth phase. Biosci Biotechnol Biochem 67:2668-2673.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 2668-2673
    • Kajiwara, H.1    Kaneko, T.2    Ishizaka, M.3    Tajima, S.4    Kouchi, H.5
  • 91
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, Hillenkamp F (1988) Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 60:2299-2301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 92
    • 5644233706 scopus 로고    scopus 로고
    • The secretome of the plant pathogenic bacterium Erwinia chrysanthemi
    • Kazemi-Pour N, Condemine G, Hugouvieux-Cotte-Pattat N (2004) The secretome of the plant pathogenic bacterium Erwinia chrysanthemi. Proteomics 4:3177-3186.
    • (2004) Proteomics , vol.4 , pp. 3177-3186
    • Kazemi-Pour, N.1    Condemine, G.2    Hugouvieux-Cotte-Pattat, N.3
  • 93
    • 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 JY, Kim S-J, Park KR, Chung H-J, Leem S-H, Kim SI (2004) Proteomic analysis of Acinetobacter lwoffii K24 by 2-D gel electrophoresis and electrospray ionization quadrupole-time of flight mass spectrometry. J Microbiol Methods 57:337-349.
    • (2004) J Microbiol Methods , vol.57 , 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
  • 95
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals
    • Klose J (1975) Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals. Humangenetik 26:231-243.
    • (1975) Humangenetik , vol.26 , pp. 231-243
    • Klose, J.1
  • 97
    • 8844232706 scopus 로고    scopus 로고
    • Functional genomics to new drug targets
    • Kramer R, Cohen D (2004) Functional genomics to new drug targets. Nat Rev Drug Discov 3:965-972.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 965-972
    • Kramer, R.1    Cohen, D.2
  • 99
    • 14544281667 scopus 로고    scopus 로고
    • Substrate-dependent regulation of anaerobic degradation pathways for toluene and ethylbenzene in a denitrifying bacterium, strain EbN1
    • Kühner S, Wöhlbrandt L, Fritz I, Wruck W, Hultschig C, Hufnagel P, Kube M, Reinhardt R, Rabus R (2005) Substrate-dependent regulation of anaerobic degradation pathways for toluene and ethylbenzene in a denitrifying bacterium, strain EbN1. J Bacteriol 187:1493-1503.
    • (2005) J Bacteriol , vol.187 , pp. 1493-1503
    • Kühner, S.1    Wöhlbrandt, L.2    Fritz, I.3    Wruck, W.4    Hultschig, C.5    Hufnagel, P.6    Kube, M.7    Reinhardt, R.8    Rabus, R.9
  • 103
    • 2442471747 scopus 로고    scopus 로고
    • Comparison of the proteome of Methylobacterium extorquens AM1 grown under methylotrophic and nonmethylotrophic conditions
    • Laukel M, Rossignol M, Borderies G, Völker U, Vorholt JA (2004) Comparison of the proteome of Methylobacterium extorquens AM1 grown under methylotrophic and nonmethylotrophic conditions. Proteomics 4:1247-1264.
    • (2004) Proteomics , vol.4 , pp. 1247-1264
    • Laukel, M.1    Rossignol, M.2    Borderies, G.3    Völker, U.4    Vorholt, J.A.5
  • 105
    • 0347132485 scopus 로고    scopus 로고
    • Escherichia coli - A model system that benefits from and contributes to the evolution of proteomics
    • Lee PS, Lee KH (2003) Escherichia coli - a model system that benefits from and contributes to the evolution of proteomics. Biotechnol Bioeng 84:801-814.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 801-814
    • Lee, P.S.1    Lee, K.H.2
  • 106
    • 0038216710 scopus 로고    scopus 로고
    • Cellular and extracellular proteome analysis of Streptococcus mutans grown in a chemostat
    • Len ACL, Cordwell SJ, Harty DWS, Jacques NA (2003) Cellular and extracellular proteome analysis of Streptococcus mutans grown in a chemostat. Proteomics 3:627-646.
    • (2003) Proteomics , vol.3 , pp. 627-646
    • Len, A.C.L.1    Cordwell, S.J.2    Harty, D.W.S.3    Jacques, N.A.4
  • 107
    • 1542373514 scopus 로고    scopus 로고
    • Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii
    • Leverrier P, Vissers JPC, Rouault A, Boyaval P, Jan G (2004) Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii. Arch Microbiol 181:215-230.
    • (2004) Arch Microbiol , vol.181 , pp. 215-230
    • Leverrier, P.1    Vissers, J.P.C.2    Rouault, A.3    Boyaval, P.4    Jan, G.5
  • 108
    • 14844326682 scopus 로고    scopus 로고
    • Proteome of Methanosarcina acetivorans. Part I: An expanded view of the biology of the cell
    • Li Q, Li L, Rejtar T, Karger BL, Ferry JG (2005) Proteome of Methanosarcina acetivorans. Part I: An expanded view of the biology of the cell. J Proteome Res 4:112-128.
    • (2005) J Proteome Res , vol.4 , pp. 112-128
    • Li, Q.1    Li, L.2    Rejtar, T.3    Karger, B.L.4    Ferry, J.G.5
  • 111
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann M, Hendrickson RC, Pandey A (2001) Analysis of proteins and proteomes by mass spectrometry. Annu Rev Biochem 70:437-473.
    • (2001) Annu Rev Biochem , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 112
    • 0028575316 scopus 로고
    • Error-tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann M, Wilm M (1994) Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal Chem 66:4390-4399.
    • (1994) Anal Chem , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 113
    • 27744466163 scopus 로고    scopus 로고
    • Isolation and characterization of a Lactobacillus helveticus ITG LH1 peptidase-rich sub-proteome
    • Manso MA, Léonil J, Piot M, Gagnaire V (2005) Isolation and characterization of a Lactobacillus helveticus ITG LH1 peptidase-rich sub-proteome. Int J Food Microbiol 105:119-129.
    • (2005) Int J Food Microbiol , vol.105 , pp. 119-129
    • Manso, M.A.1    Léonil, J.2    Piot, M.3    Gagnaire, V.4
  • 115
    • 21244495253 scopus 로고    scopus 로고
    • The development of the DIGE system: 2D fluorescence difference gel analysis technology
    • Marouga R, David S, Hawkins E (2005) The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal Bioanal Chem 382:669-678.
    • (2005) Anal Bioanal Chem , vol.382 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 119
    • 0242523637 scopus 로고    scopus 로고
    • Approaches for the quantification of protein concentration ratios
    • Moritz B, Meyer HE (2003) Approaches for the quantification of protein concentration ratios. Proteomics 3:2208-2220.
    • (2003) Proteomics , vol.3 , pp. 2208-2220
    • Moritz, B.1    Meyer, H.E.2
  • 121
    • 0036024975 scopus 로고    scopus 로고
    • Blue Native electrophoresis to study mitochondrial and other protein complexes
    • Nijtmans LGJ, Henderson NS, Holt IJ (2002) Blue Native electrophoresis to study mitochondrial and other protein complexes. Methods 26:327-334.
    • (2002) Methods , vol.26 , pp. 327-334
    • Nijtmans, L.G.J.1    Henderson, N.S.2    Holt, I.J.3
  • 122
    • 18844464043 scopus 로고    scopus 로고
    • Global analysis of the Ralstonia metallidurans proteome: Prelude for the large-scale study of heavy metal response
    • Noël-Georis I, Vallaeys T, Chauvaux R, Monchy S, Falmagne P, Mergeay M, Wattiez R (2004) Global analysis of the Ralstonia metallidurans proteome: prelude for the large-scale study of heavy metal response. Proteomics 4:151-179.
    • (2004) Proteomics , vol.4 , pp. 151-179
    • Noël-Georis, I.1    Vallaeys, T.2    Chauvaux, R.3    Monchy, S.4    Falmagne, P.5    Mergeay, M.6    Wattiez, R.7
  • 123
    • 0034855587 scopus 로고    scopus 로고
    • Large-gel two-dimensional electrophoresis-matrix assisted laser desorption/ionization-time of flight-mass spectrometry: An analytical challenge for studying complex protein mixtures
    • Nordhoff E, Egelhofer V, Giavalisco P, Eickhoff H, Horn M, Przewieslik T, Theiss D, Schneider U, Lehrach H, Gobom J (2001) Large-gel two-dimensional electrophoresis-matrix assisted laser desorption/ionization-time of flight-mass spectrometry: an analytical challenge for studying complex protein mixtures. Electrophoresis 22:2844-2855.
    • (2001) Electrophoresis , vol.22 , pp. 2844-2855
    • Nordhoff, E.1    Egelhofer, V.2    Giavalisco, P.3    Eickhoff, H.4    Horn, M.5    Przewieslik, T.6    Theiss, D.7    Schneider, U.8    Lehrach, H.9    Gobom, J.10
  • 124
    • 0036744393 scopus 로고    scopus 로고
    • Proteomic comparison of membrane and extracellular proteins from invasive (PAO1) and cytotoxic (6206) strains of Pseudomonas aeruginosa
    • Nouwens AS, Willcox MDP, Walsh BJ, Cordwell SJ (2002) Proteomic comparison of membrane and extracellular proteins from invasive (PAO1) and cytotoxic (6206) strains of Pseudomonas aeruginosa. Proteomics 2:1325-1346.
    • (2002) Proteomics , vol.2 , pp. 1325-1346
    • Nouwens, A.S.1    Willcox, M.D.P.2    Walsh, B.J.3    Cordwell, S.J.4
  • 125
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • USA
    • Oda Y, Huang K, Cross FR, Cowburn D, Chait BT (1999) Accurate quantitation of protein expression and site-specific phosphorylation. Proc Natl Acad Sci USA 96:6591-6596.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 126
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007-4021.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 127
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • 3.6
    • Olsen JV, Ong S-E, Mann M (2004) Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol Cell Proteomics 3.6:608-614.
    • (2004) Mol Cell Proteomics , pp. 608-614
    • Olsen, J.V.1    Ong, S.-E.2    Mann, M.3
  • 128
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • 1.5
    • Ong S-E, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1.5:376-386.
    • (2002) Mol Cell Proteomics , 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
  • 130
    • 2942587229 scopus 로고    scopus 로고
    • Cross-species identification of proteins from proteome profiles of the marine oligotrophic ultra-microbacterium, Sphingopyxis alaskensis
    • Ostrowski M, Fegatella F, Wasinger V, Guilhaus M, Corthals GL, Cavicchioli R (2004) Cross-species identification of proteins from proteome profiles of the marine oligotrophic ultra-microbacterium, Sphingopyxis alaskensis. Proteomics 4:1779-1788.
    • (2004) Proteomics , vol.4 , pp. 1779-1788
    • Ostrowski, M.1    Fegatella, F.2    Wasinger, V.3    Guilhaus, M.4    Corthals, G.L.5    Cavicchioli, R.6
  • 132
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin DJ, Hojrup P, Bleasby AJ (1993) Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 3:327-332.
    • (1993) Curr Biol , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 133
    • 1542543814 scopus 로고    scopus 로고
    • Reference map of soluble proteins from Salmonella enterica serovar enteritidis by two-dimensional electrophoresis
    • Park M-R, Lee E-G, Kim Y-H, Jung T-S, Shin Y-S, Shin G-W, Cha H-G, Kim G-S (2003) Reference map of soluble proteins from Salmonella enterica serovar enteritidis by two-dimensional electrophoresis. J Vet Sci 4:143-149.
    • (2003) J Vet Sci , vol.4 , pp. 143-149
    • Park, M.-R.1    Lee, E.-G.2    Kim, Y.-H.3    Jung, T.-S.4    Shin, Y.-S.5    Shin, G.-W.6    Cha, H.-G.7    Kim, G.-S.8
  • 134
    • 27644446855 scopus 로고    scopus 로고
    • Global physiological understanding and metabolic engineering of microorganisms based on omics studies
    • doi 10.1007/s00253-005-0081-z
    • Park SJ, Lee SY, Cho J, Kim TY, Lee JW, Park JH, Han M-J (2005) Global physiological understanding and metabolic engineering of microorganisms based on omics studies. Appl Microbiol Biotechnol (doi 10.1007/s00253-005-0081-z).
    • (2005) Appl Microbiol Biotechnol
    • Park, S.J.1    Lee, S.Y.2    Cho, J.3    Kim, T.Y.4    Lee, J.W.5    Park, J.H.6    Han, M.-J.7
  • 135
    • 0026508210 scopus 로고
    • A mechanically strong matrix for protein electrophoresis with enhanced silver staining properties
    • Patton WF, Lopez MF, Barry P, Skea WM (1992) A mechanically strong matrix for protein electrophoresis with enhanced silver staining properties. Biotechniques 12:580-585.
    • (1992) Biotechniques , vol.12 , pp. 580-585
    • Patton, W.F.1    Lopez, M.F.2    Barry, P.3    Skea, W.M.4
  • 136
    • 0017861127 scopus 로고
    • Patterns of protein synthesis in E. coli: A catalog of the amount of 140 individual proteins at different growth rates
    • Pedersen S, Bloch PL, Reeh S, Neidhardt FC (1978) Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates. Cell 14:179-190.
    • (1978) Cell , vol.14 , pp. 179-190
    • Pedersen, S.1    Bloch, P.L.2    Reeh, S.3    Neidhardt, F.C.4
  • 138
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J Proteome Res 2:43-50.
    • (2003) J Proteome Res , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 139
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJC, Creasy DM, Cottrell JS (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 142
    • 0029742635 scopus 로고    scopus 로고
    • Proteome of Salmonella typhimurium SL1344: Identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map
    • Qi S-Y, Moir A, O'Connor CD (1996) Proteome of Salmonella typhimurium SL1344: identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map. J Bacteriol 178:5032-5038.
    • (1996) J Bacteriol , vol.178 , pp. 5032-5038
    • Qi, S.-Y.1    Moir, A.2    O'Connor, C.D.3
  • 143
    • 2342628481 scopus 로고    scopus 로고
    • Data standards for 'omic' science
    • Quackenbush J (2004) Data standards for 'omic' science. Nat Biotechnol 22:613-614.
    • (2004) Nat Biotechnol , vol.22 , pp. 613-614
    • Quackenbush, J.1
  • 144
    • 27644514544 scopus 로고    scopus 로고
    • Biodegradation of hydrocarbons under anoxic conditions
    • Ollivier B, Magot M (eds): Washington DC, ASM Press
    • Rabus R (2005a) Biodegradation of hydrocarbons under anoxic conditions; in Ollivier B, Magot M (eds): Petroleum Microbiology. Washington DC, ASM Press, pp 277-299.
    • (2005) Petroleum Microbiology , pp. 277-299
    • Rabus, R.1
  • 145
    • 27644578460 scopus 로고    scopus 로고
    • Functional genomics of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1
    • Rabus R (2005b) Functional genomics of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1. Appl Microbiol Biotechnol 68:580-587.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 580-587
    • Rabus, R.1
  • 146
    • 0036428728 scopus 로고    scopus 로고
    • Genes involved in the anaerobic degradation of ethylbenzene in a denitrifying bacterium, strain EbN1
    • Rabus R, Kube M, Beck A, Widdel F, Reinhardt R (2002) Genes involved in the anaerobic degradation of ethylbenzene in a denitrifying bacterium, strain EbN1. Arch Microbiol 178:506-516.
    • (2002) Arch Microbiol , vol.178 , pp. 506-516
    • Rabus, R.1    Kube, M.2    Beck, A.3    Widdel, F.4    Reinhardt, R.5
  • 148
    • 0028920232 scopus 로고
    • Anaerobic degradation of ethylbenzene and other aromatic hydrocarbons by new denitrifying bacteria
    • Rabus R, Widdel F (1995) Anaerobic degradation of ethylbenzene and other aromatic hydrocarbons by new denitrifying bacteria. Arch Microbiol 163:96-103.
    • (1995) Arch Microbiol , vol.163 , pp. 96-103
    • Rabus, R.1    Widdel, F.2
  • 149
    • 0029930415 scopus 로고    scopus 로고
    • Utilization of alkylbenzenes during anaerobic growth of pure cultures of denitrifying bacteria on crude oil
    • Rabus R, Widdel F (1996) Utilization of alkylbenzenes during anaerobic growth of pure cultures of denitrifying bacteria on crude oil. Appl Environ Microbiol 62:1238-1241.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1238-1241
    • Rabus, R.1    Widdel, F.2
  • 151
    • 4143137531 scopus 로고    scopus 로고
    • Differential protein expression during growth of Acidithiobacillus ferrooxidans on ferrous iron, sulfur compounds, or metal sulfides
    • Ramírez P, Guiliani N, Valenzuela L, Beard S, Jerez CA (2004) Differential protein expression during growth of Acidithiobacillus ferrooxidans on ferrous iron, sulfur compounds, or metal sulfides. Appl Environ Microbiol 70:4491-4498.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 4491-4498
    • Ramírez, P.1    Guiliani, N.2    Valenzuela, L.3    Beard, S.4    Jerez, C.A.5
  • 152
    • 0038655411 scopus 로고    scopus 로고
    • Development of Listeria monocytogenes EGDe partial proteome reference map and comparison with the protein profiles of food isolates
    • Ramnath M, Rechinger KB, Jänsch L, Hastings JW, Knøchel S, Gravesen A (2003) Development of Listeria monocytogenes EGDe partial proteome reference map and comparison with the protein profiles of food isolates. Appl Environ Microbiol 69:3368-3376.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3368-3376
    • Ramnath, M.1    Rechinger, K.B.2    Jänsch, L.3    Hastings, J.W.4    Knøchel, S.5    Gravesen, A.6
  • 153
    • 21444457837 scopus 로고    scopus 로고
    • Toward data standards for proteomics
    • Ravichandran V, Sriram RD (2005) Toward data standards for proteomics. Nat Biotechnol 23:373-376.
    • (2005) Nat Biotechnol , vol.23 , pp. 373-376
    • Ravichandran, V.1    Sriram, R.D.2
  • 154
    • 17144394372 scopus 로고    scopus 로고
    • Proteome analysis of Rickettsia conorii by two-dimensional gel electrophoresis coupled with mass spectrometry
    • Renesto P, Azza S, Dolla A, Fourquet P, Vestris G, Gorvel J-P, Raoult D (2005) Proteome analysis of Rickettsia conorii by two-dimensional gel electrophoresis coupled with mass spectrometry. FEMS Microbiol Lett 245:231-238.
    • (2005) FEMS Microbiol Lett , vol.245 , pp. 231-238
    • Renesto, P.1    Azza, S.2    Dolla, A.3    Fourquet, P.4    Vestris, G.5    Gorvel, J.-P.6    Raoult, D.7
  • 156
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff P, Fohlman J (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed Mass Spectrom 11:601.
    • (1984) Biomed Mass Spectrom , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 160
    • 18744398125 scopus 로고    scopus 로고
    • Large-scale database searching using tandem mass spectra: Looking up the answer in the back of the book
    • Sadygov RG, Cociorva D, Yates 3rd JR (2004) Large-scale database searching using tandem mass spectra: looking up the answer in the back of the book. Nat Methods 1:195-202.
    • (2004) Nat Methods , vol.1 , pp. 195-202
    • Sadygov, R.G.1    Cociorva, D.2    Yates III, J.R.3
  • 161
    • 0032877281 scopus 로고    scopus 로고
    • Cyno2Dbase updated: Linkage of 234 protein spots to corresponding genes through N-terminal microsequencing
    • Sazuka T, Yamaguchi M, Ohara O (1999) Cyno2Dbase updated: linkage of 234 protein spots to corresponding genes through N-terminal microsequencing. Electrophoresis 20:2160-2171.
    • (1999) Electrophoresis , vol.20 , pp. 2160-2171
    • Sazuka, T.1    Yamaguchi, M.2    Ohara, O.3
  • 163
    • 0028806048 scopus 로고
    • Quantitative monitoring of gene expression patterns with a complementary DNA microarray
    • Schena M, Shalon D, Davis RW, Brown PO (1995) Quantitative monitoring of gene expression patterns with a complementary DNA microarray. Science 270:467-470.
    • (1995) Science , vol.270 , pp. 467-470
    • Schena, M.1    Shalon, D.2    Davis, R.W.3    Brown, P.O.4
  • 164
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • Schmidt A, Kellermann J, Lottspeich F (2005a) A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics 5:4-15.
    • (2005) Proteomics , vol.5 , pp. 4-15
    • Schmidt, A.1    Kellermann, J.2    Lottspeich, F.3
  • 165
    • 20844463020 scopus 로고    scopus 로고
    • Global whole-cell FTICR mass spectrometric proteomics analysis of the heat shock response in the radioresistant bacterium Deinococcus radiodurans
    • Schmid AK, Lipton MS, Mottaz H, Monroe ME, Smith RD, Lidstrom ME (2005a) Global whole-cell FTICR mass spectrometric proteomics analysis of the heat shock response in the radioresistant bacterium Deinococcus radiodurans. J Proteome Res 4:709-718.
    • (2005) J Proteome Res , vol.4 , pp. 709-718
    • Schmid, A.K.1    Lipton, M.S.2    Mottaz, H.3    Monroe, M.E.4    Smith, R.D.5    Lidstrom, M.E.6
  • 167
    • 0043166916 scopus 로고    scopus 로고
    • An improved mechanically durable electrophoresis gel matrix that is fully compatible with fluorescence-based protein detection technologies
    • Schulenberg B, Arnold B, Patton WF (2003) An improved mechanically durable electrophoresis gel matrix that is fully compatible with fluorescence-based protein detection technologies. Proteomics 3:1196-1205.
    • (2003) Proteomics , vol.3 , pp. 1196-1205
    • Schulenberg, B.1    Arnold, B.2    Patton, W.F.3
  • 171
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes
    • Shaw J, Rowlinson R, Nickson J, Stone T, Sweet A, Williams K, Tonge R (2003) Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes. Proteomics 3:1181-1195.
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Rowlinson, R.2    Nickson, J.3    Stone, T.4    Sweet, A.5    Williams, K.6    Tonge, R.7
  • 172
    • 0030960366 scopus 로고    scopus 로고
    • Rapid de novo peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko A, Chernushevich I, Ens W, Standing KG, Thomson B, Wilm M, Mann M (1997) Rapid de novo peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun Mass Spectrom 11:1015-1024.
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 173
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko A, Sunyaev S, Loboda A, Shevchenko A, Bork P, Ens W, Standing KG (2001) Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal Chem 73:1917-1926.
    • (2001) Anal Chem , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.G.7
  • 174
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 175
  • 181
    • 0037015858 scopus 로고    scopus 로고
    • Gene homology resources on the World Wide Web
    • Turchin A, Kohane IS (2002) Gene homology resources on the World Wide Web. Physiol Genomics 11:165-177.
    • (2002) Physiol Genomics , vol.11 , pp. 165-177
    • Turchin, A.1    Kohane, I.S.2
  • 183
    • 0035987510 scopus 로고    scopus 로고
    • The proteome of the bacterium Mycoplasma pneumoniae: Comparing predicted open reading frames to identified gene products
    • Ueberle B, Frank R, Herrmann R (2002) The proteome of the bacterium Mycoplasma pneumoniae: comparing predicted open reading frames to identified gene products. Proteomics 2:754-764.
    • (2002) Proteomics , vol.2 , pp. 754-764
    • Ueberle, B.1    Frank, R.2    Herrmann, R.3
  • 184
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Ünlü M, Morgan ME, Minden JS (1997) Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18:2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Ünlü, M.1    Morgan, M.E.2    Minden, J.S.3
  • 185
    • 14744293536 scopus 로고    scopus 로고
    • Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra
    • Venable JD, Dong M-Q, Wohlschlegel J, Dillin A, Yates 3rd JR (2004) Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra. Nat Methods 1:1-7.
    • (2004) Nat Methods , vol.1 , pp. 1-7
    • Venable, J.D.1    Dong, M.-Q.2    Wohlschlegel, J.3    Dillin, A.4    Yates III, J.R.5
  • 189
    • 0000094029 scopus 로고
    • Improved resolution and very high sensitivity in MALDI TOF of matrix surfaces made by fast evaporation
    • Vorm O, Roepstroff P, Mann M (1994) Improved resolution and very high sensitivity in MALDI TOF of matrix surfaces made by fast evaporation. Anal Chem 66:3281-3287.
    • (1994) Anal Chem , vol.66 , pp. 3281-3287
    • Vorm, O.1    Roepstroff, P.2    Mann, M.3
  • 191
    • 23744515352 scopus 로고    scopus 로고
    • Mass spectrometry of the M. smegmatis proteome: Protein expression levels correlate with function, operons, and codon bias
    • Wang R, Prince JT, Marcotte EM (2005) Mass spectrometry of the M. smegmatis proteome: protein expression levels correlate with function, operons, and codon bias. Genome Res 15:1118-1126.
    • (2005) Genome Res , vol.15 , pp. 1118-1126
    • Wang, R.1    Prince, J.T.2    Marcotte, E.M.3
  • 192
    • 0042367748 scopus 로고    scopus 로고
    • Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae
    • Wang W, Sun J, Hartlep M, Deckwer W-D, Zeng A-P (2003) Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae. Biotechnol Bioeng 83:525-536.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 525-536
    • Wang, W.1    Sun, J.2    Hartlep, M.3    Deckwer, W.-D.4    Zeng, A.-P.5
  • 194
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates 3rd JR (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 195
    • 13244249605 scopus 로고    scopus 로고
    • Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100
    • Watt SA, Wilke A, Patschkowski T, Niehaus K (2005) Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100. Proteomics 5:153-167.
    • (2005) Proteomics , vol.5 , pp. 153-167
    • Watt, S.A.1    Wilke, A.2    Patschkowski, T.3    Niehaus, K.4
  • 196
    • 0035370088 scopus 로고    scopus 로고
    • Anaerobic biodegradation of saturated and aromatic hydrocarbons
    • Widdel F, Rabus R (2001) Anaerobic biodegradation of saturated and aromatic hydrocarbons. Curr Opin Biotechnol 12:259-276.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 259-276
    • Widdel, F.1    Rabus, R.2
  • 198
    • 0034213595 scopus 로고    scopus 로고
    • ProFound: An expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang W, Chait BT (2000) ProFound: an expert system for protein identification using mass spectrometric peptide mapping information. Anal Chem 72:2482-2489.
    • (2000) Anal Chem , vol.72 , pp. 2482-2489
    • Zhang, W.1    Chait, B.T.2
  • 199
    • 13244252298 scopus 로고    scopus 로고
    • Differential protein expression by Porphyromonas gingivalis in response to secreted epithelial cell components
    • Zhang Y, Wang T, Chen W, Yilmaz Ö, Park Y, Jung I-Y, Hackett M, Lamont RJ (2005) Differential protein expression by Porphyromonas gingivalis in response to secreted epithelial cell components. Proteomics 5:198-211.
    • (2005) Proteomics , vol.5 , pp. 198-211
    • Zhang, Y.1    Wang, T.2    Chen, W.3    Yilmaz, Ö.4    Park, Y.5    Jung, I.-Y.6    Hackett, M.7    Lamont, R.J.8
  • 200
    • 18844410520 scopus 로고    scopus 로고
    • 54 in response to gentisate induction in Pseudomonas alcaligenes NCIMB 9867
    • 54 in response to gentisate induction in Pseudomonas alcaligenes NCIMB 9867. Proteomics 5:1868-1876.
    • (2005) Proteomics , vol.5 , pp. 1868-1876
    • Zhao, B.1    Yeo, C.C.2    Poh, C.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.