메뉴 건너뛰기




Volumn 13, Issue 8, 2011, Pages 1934-1955

Proteomics of extremophiles

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 80051926124     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/j.1462-2920.2011.02484.x     Document Type: Short Survey
Times cited : (22)

References (265)
  • 1
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold, R., and Goodlett, D.R. (2001) Mass spectrometry in proteomics. Chem Rev 101: 269-296.
    • (2001) Chem Rev , vol.101 , pp. 269-296
    • Aebersold, R.1    Goodlett, D.R.2
  • 2
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422: 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 32144446968 scopus 로고    scopus 로고
    • Alignment and statistical difference analysis of complex peptide data sets generated by multidimensional LC-MS
    • America, A., Cordewener, J., van Geffen, M., Lommen, A., Vissers, J., Bino, R., and Hall, R. (2006) Alignment and statistical difference analysis of complex peptide data sets generated by multidimensional LC-MS. Proteomics 6: 641-653.
    • (2006) Proteomics , vol.6 , pp. 641-653
    • America, A.1    Cordewener, J.2    van Geffen, M.3    Lommen, A.4    Vissers, J.5    Bino, R.6    Hall, R.7
  • 6
    • 77955096719 scopus 로고    scopus 로고
    • Thermoacidophiles and their protein adaptation to low pH and high temperature
    • In Siddiqui, K.S., and Thomas, T. (eds). New York: Nova biomedical books
    • Antranikian, G. (2008) Thermoacidophiles and their protein adaptation to low pH and high temperature. In Protein Adaptation in Extremophiles. Siddiqui, K.S., and Thomas, T. (eds). New York: Nova biomedical books, pp. 143-146.
    • (2008) Protein Adaptation in Extremophiles , pp. 143-146
    • Antranikian, G.1
  • 8
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D., and Varshavsky, A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 9
    • 0037069421 scopus 로고    scopus 로고
    • Coordinate regulation of energy transduction modules in Halobacterium sp. Analyzed by a global systems approach
    • Baliga, N.S., Pan, M., Goo, Y.A., Yi, E.C., Goodlett, D.R., Dimitrov, K., etal. (2002) Coordinate regulation of energy transduction modules in Halobacterium sp. Analyzed by a global systems approach. Proc Natl Acad Sci USA 99: 14913-14918.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14913-14918
    • Baliga, N.S.1    Pan, M.2    Goo, Y.A.3    Yi, E.C.4    Goodlett, D.R.5    Dimitrov, K.6
  • 10
    • 32544431583 scopus 로고    scopus 로고
    • Proteogenomic approaches for the molecular characterization of natural microbial communities
    • Banfield, J.F., VerBerkmoes, N.C., Hettich, R.L., and Thelen, M.P. (2005) Proteogenomic approaches for the molecular characterization of natural microbial communities. OMICS 4: 301-333.
    • (2005) OMICS , vol.4 , pp. 301-333
    • Banfield, J.F.1    VerBerkmoes, N.C.2    Hettich, R.L.3    Thelen, M.P.4
  • 11
  • 12
    • 33746674380 scopus 로고    scopus 로고
    • Proteomic mapping of the hyperthermophilic and acidophilic archaeon Solfolobus solfataricus p2
    • Barry, R.C., Young, M.J., Stedman, K.M., and Dratz, E.A. (2006) Proteomic mapping of the hyperthermophilic and acidophilic archaeon Solfolobus solfataricus p2. Electrophoresis 27: 2970-2983.
    • (2006) Electrophoresis , vol.27 , pp. 2970-2983
    • Barry, R.C.1    Young, M.J.2    Stedman, K.M.3    Dratz, E.A.4
  • 13
    • 73149103678 scopus 로고    scopus 로고
    • Soil metaproteomics: a review of an emerging environmental science. Significance, methodology and perspectives
    • Bastida, F., Moreno, J.L., Nicolas, C., Hernandez, T., and Garcia, C. (2009) Soil metaproteomics: a review of an emerging environmental science. Significance, methodology and perspectives. Eur J Soil Sci 60: 845-859.
    • (2009) Eur J Soil Sci , vol.60 , pp. 845-859
    • Bastida, F.1    Moreno, J.L.2    Nicolas, C.3    Hernandez, T.4    Garcia, C.5
  • 14
    • 33748377124 scopus 로고    scopus 로고
    • Quantification of protein half-lives in the budding yeast proteome
    • Belle, A., Tanay, A., Bitincka, L., Shamir, R., and O'Shea, E.K. (2006) Quantification of protein half-lives in the budding yeast proteome. Proc Natl Acad Sci USA 103: 13004-13009.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13004-13009
    • Belle, A.1    Tanay, A.2    Bitincka, L.3    Shamir, R.4    O'Shea, E.K.5
  • 15
    • 34547347640 scopus 로고    scopus 로고
    • Functional metaproteome analysis of protein extracts from contaminated soil and groundwater
    • Benndorf, D., Balcke, G.U., Harms, H., and Bergen, M.V. (2007) Functional metaproteome analysis of protein extracts from contaminated soil and groundwater. ISME J 1: 224-234.
    • (2007) ISME J , vol.1 , pp. 224-234
    • Benndorf, D.1    Balcke, G.U.2    Harms, H.3    Bergen, M.V.4
  • 16
    • 0022820166 scopus 로고
    • Mass spectrometry methods for protein sequencing
    • Biemann, K. (1986) Mass spectrometry methods for protein sequencing. Anal Chem 58: 1288A-1300A.
    • (1986) Anal Chem , vol.58
    • Biemann, K.1
  • 17
    • 33750601062 scopus 로고    scopus 로고
    • The pitfalls of proteomics experiments without the correct use of bioinformatics tools
    • Biron, D.G., Brun, C., Lefevre, T., Lebarbenchon, C., Loxdale, H.D., Chevenet, F., etal. (2006) The pitfalls of proteomics experiments without the correct use of bioinformatics tools. Proteomics 6: 5577-5596.
    • (2006) Proteomics , vol.6 , pp. 5577-5596
    • Biron, D.G.1    Brun, C.2    Lefevre, T.3    Lebarbenchon, C.4    Loxdale, H.D.5    Chevenet, F.6
  • 19
    • 51649102828 scopus 로고    scopus 로고
    • A shotgun proteomic method for the identification of membrane-embedded proteins and peptides
    • Blackler, A.R., Speers, A.E., Ladinsky, M.S., and Wu, C.C. (2008) A shotgun proteomic method for the identification of membrane-embedded proteins and peptides. J Proteome Res 7: 3028-3034.
    • (2008) J Proteome Res , vol.7 , pp. 3028-3034
    • Blackler, A.R.1    Speers, A.E.2    Ladinsky, M.S.3    Wu, C.C.4
  • 20
    • 12144291497 scopus 로고    scopus 로고
    • Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling
    • Blondeau, F., Ritter, B., Allaire, P., Wasiak, S., Girard, M., Hussain, N., etal. (2004) Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling. Proc Natl Acad Sci USA 101: 3833-3838.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3833-3838
    • Blondeau, F.1    Ritter, B.2    Allaire, P.3    Wasiak, S.4    Girard, M.5    Hussain, N.6
  • 21
    • 0036665518 scopus 로고    scopus 로고
    • Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry
    • Blonder, J., Goshe, M.B., Moore, R.J., Pasa-Tolic, L., Masselon, C.D., Lipton, M.S., and Smith, R.D. (2002) Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry. J Proteome Res 1: 351-360.
    • (2002) J Proteome Res , vol.1 , pp. 351-360
    • Blonder, J.1    Goshe, M.B.2    Moore, R.J.3    Pasa-Tolic, L.4    Masselon, C.D.5    Lipton, M.S.6    Smith, R.D.7
  • 22
    • 0942276251 scopus 로고    scopus 로고
    • A detergent- and cyanogen bromide-free method for integral membrane proteomics: application to halobacterium purple membranes and the human epidermal membrane proteome
    • Blonder, J., Conrads, T.P., Yu, L.R., Terunuma, A., Janini, G.M., Issaq, H.J., etal. (2004a) A detergent- and cyanogen bromide-free method for integral membrane proteomics: application to halobacterium purple membranes and the human epidermal membrane proteome. Proteomics 4: 31-45.
    • (2004) Proteomics , vol.4 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.R.3    Terunuma, A.4    Janini, G.M.5    Issaq, H.J.6
  • 23
    • 4444245486 scopus 로고    scopus 로고
    • Global analysis of the membrane subproteome of Pseudomonas aeruginosa using liquid chromatography-tandem mass spectrometry
    • Blonder, J., Goshe, M.B., Xiao, W., Camp, D.G., 2nd, Wingerd, M., Davis, R.W., and Smith, R.D. (2004b) Global analysis of the membrane subproteome of Pseudomonas aeruginosa using liquid chromatography-tandem mass spectrometry. J Proteome Res 3: 434-444.
    • (2004) J Proteome Res , vol.3 , pp. 434-444
    • Blonder, J.1    Goshe, M.B.2    Xiao, W.3    Camp 2nd, D.G.4    Wingerd, M.5    Davis, R.W.6    Smith, R.D.7
  • 24
    • 4644252123 scopus 로고    scopus 로고
    • A proteomic characterization of the plasma membrane of human epidermis by high-throughput mass spectrometry
    • Blonder, J., Terunuma, A., Conrads, T.P., Chan, K.C., Yee, C., Lucas, D.A., etal. (2004c) A proteomic characterization of the plasma membrane of human epidermis by high-throughput mass spectrometry. J Invest Dermatol 123: 691-699.
    • (2004) J Invest Dermatol , vol.123 , pp. 691-699
    • Blonder, J.1    Terunuma, A.2    Conrads, T.P.3    Chan, K.C.4    Yee, C.5    Lucas, D.A.6
  • 26
    • 0037434977 scopus 로고    scopus 로고
    • Biomedical informatics for proteomics
    • Boguski, M.S., and McIntosh, M.W. (2003) Biomedical informatics for proteomics. Nature 422: 233-237.
    • (2003) Nature , vol.422 , pp. 233-237
    • Boguski, M.S.1    McIntosh, M.W.2
  • 27
    • 0037106398 scopus 로고    scopus 로고
    • Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry
    • Bondarenko, P., Chelius, D., and Shaler, T. (2002) Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Anal Chem 74: 4741-4749.
    • (2002) Anal Chem , vol.74 , pp. 4741-4749
    • Bondarenko, P.1    Chelius, D.2    Shaler, T.3
  • 28
    • 34848925460 scopus 로고    scopus 로고
    • Mascot file parsing and quantification (MFPaQ), a new software to parse, validate, and quantify proteomic data generated by ICAT and SILAC mass spectrometric analyses: application to the proteomic study of membrane proteins from primary human endothelial cells
    • Bouyssie, D., de Peredo, G., Mouton, E., Albigot, R., Roussel, L., Ortega, N., etal. (2007) Mascot file parsing and quantification (MFPaQ), a new software to parse, validate, and quantify proteomic data generated by ICAT and SILAC mass spectrometric analyses: application to the proteomic study of membrane proteins from primary human endothelial cells. Mol Cell Proteomics 9: 1621-1637.
    • (2007) Mol Cell Proteomics , vol.9 , pp. 1621-1637
    • Bouyssie, D.1    de Peredo, G.2    Mouton, E.3    Albigot, R.4    Roussel, L.5    Ortega, N.6
  • 29
    • 67649511917 scopus 로고    scopus 로고
    • Isotope dilution strategies for absolute quantitative proteomics
    • Brun, V., Masselon, C., Garin, J., and Dupuis, A. (2009) Isotope dilution strategies for absolute quantitative proteomics. J Proteomics 72: 740-749.
    • (2009) J Proteomics , vol.72 , pp. 740-749
    • Brun, V.1    Masselon, C.2    Garin, J.3    Dupuis, A.4
  • 30
    • 33645108507 scopus 로고    scopus 로고
    • Adaptation of Bacillus subtilis to growth at low temperature: a combined transcriptomic and proteomic appraisal
    • Budde, I., Steil, L., Scharf, C., Volker, U., and Bremer, E. (2006) Adaptation of Bacillus subtilis to growth at low temperature: a combined transcriptomic and proteomic appraisal. Microbiology 152: 831-853.
    • (2006) Microbiology , vol.152 , pp. 831-853
    • Budde, I.1    Steil, L.2    Scharf, C.3    Volker, U.4    Bremer, E.5
  • 31
    • 76149132993 scopus 로고    scopus 로고
    • Analyzing the hydrophobic proteome of the Antarctic archaeon Methanococcoides burtonii using differential solubility fractionation
    • Burg, D.W., Lauro, F.M., Williams, T.J., Raftery, M.J., Guilhaus, M., and Cavicchioli, R. (2010) Analyzing the hydrophobic proteome of the Antarctic archaeon Methanococcoides burtonii using differential solubility fractionation. J Proteome Res 9: 664-676.
    • (2010) J Proteome Res , vol.9 , pp. 664-676
    • Burg, D.W.1    Lauro, F.M.2    Williams, T.J.3    Raftery, M.J.4    Guilhaus, M.5    Cavicchioli, R.6
  • 32
    • 80051911251 scopus 로고    scopus 로고
    • Temperature-dependent global gene expression in the Antarctic archaeon Methanococcoides burtonii
    • (in press): doi:10.1111/j.1462-2920.2010.02367.x.
    • Campanaro, S., Williams, T.J., Burg, D.W., De Francisci, D., Treu, L., Lauro, F.M., and Cavicchioli, R. (2010) Temperature-dependent global gene expression in the Antarctic archaeon Methanococcoides burtonii. Environ Microbiol (in press): doi:10.1111/j.1462-2920.2010.02367.x.
    • (2010) Environ Microbiol
    • Campanaro, S.1    Williams, T.J.2    Burg, D.W.3    De Francisci, D.4    Treu, L.5    Lauro, F.M.6    Cavicchioli, R.7
  • 33
    • 42049115116 scopus 로고    scopus 로고
    • Computational proteomics: management and analysis of proteomics data
    • Cannataro, M. (2008) Computational proteomics: management and analysis of proteomics data. Brief Bioinform 9: 97-101.
    • (2008) Brief Bioinform , vol.9 , pp. 97-101
    • Cannataro, M.1
  • 34
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data: working group on publication guidelines for peptide and identification data
    • Carr, S., Aebersold, R., Baldwin, M., Burlingame, A., Clauser, K., and Nesvizhskii, A. (2004) The need for guidelines in publication of peptide and protein identification data: working group on publication guidelines for peptide and identification data. Mol Cell Proteomics 3: 531-533.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4    Clauser, K.5    Nesvizhskii, A.6
  • 35
    • 0037669304 scopus 로고    scopus 로고
    • Extremophiles and the search for extra-terrestrial life
    • Cavicchioli, R. (2002) Extremophiles and the search for extra-terrestrial life. Astrobiology 2: 281-292.
    • (2002) Astrobiology , vol.2 , pp. 281-292
    • Cavicchioli, R.1
  • 38
    • 14944386094 scopus 로고    scopus 로고
    • Gel-based proteomics: what does MCP expect?
    • Celis, J.E. (2004) Gel-based proteomics: what does MCP expect? Mol Cell Proteomics 3: 949.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 949
    • Celis, J.E.1
  • 39
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • Chelius, D., and Bondarenko, P.V. (2002) Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. J Proteome Res 1: 317-323.
    • (2002) J Proteome Res , vol.1 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 41
    • 33846926966 scopus 로고    scopus 로고
    • Amino acid-coded tagging approaches in quantitative proteomics
    • Chen, X., Sun, L., Yu, Y., Xue, Y., and Yang, P. (2007) Amino acid-coded tagging approaches in quantitative proteomics. Expert Rev Proteomics 4: 25-37.
    • (2007) Expert Rev Proteomics , vol.4 , pp. 25-37
    • Chen, X.1    Sun, L.2    Yu, Y.3    Xue, Y.4    Yang, P.5
  • 43
    • 34047109199 scopus 로고    scopus 로고
    • Statistics for proteomics: experimental design and 2-DE differential analysis
    • Chich, J.-F., David, O., Villers, F., Schaeffer, B., Lutomski, D., and Huet, S. (2007) Statistics for proteomics: experimental design and 2-DE differential analysis. J Chromatogr B 849: 261-272.
    • (2007) J Chromatogr B , vol.849 , pp. 261-272
    • Chich, J.-F.1    David, O.2    Villers, F.3    Schaeffer, B.4    Lutomski, D.5    Huet, S.6
  • 44
    • 35648942133 scopus 로고    scopus 로고
    • 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for alzheimer's disease
    • Choe, L., D'Ascenzo, M., Relkin, N., Pappin, D., Ross, P., Williamson, B., etal. (2007) 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for alzheimer's disease. Proteomics 7: 3651-3660.
    • (2007) Proteomics , vol.7 , pp. 3651-3660
    • Choe, L.1    D'Ascenzo, M.2    Relkin, N.3    Pappin, D.4    Ross, P.5    Williamson, B.6
  • 45
    • 26844547984 scopus 로고    scopus 로고
    • Identification and characterization of the Sulfolobus solfataricus p2 proteome
    • Chong, P.K., Wright, P.C., Gan, C.S., and Pham, T.K. (2005) Identification and characterization of the Sulfolobus solfataricus p2 proteome. J Proteome Res 4: 1789-1798.
    • (2005) J Proteome Res , vol.4 , pp. 1789-1798
    • Chong, P.K.1    Wright, P.C.2    Gan, C.S.3    Pham, T.K.4
  • 48
    • 0034056940 scopus 로고    scopus 로고
    • The dynamic range of protein expression: a challenge for proteomic research
    • Corthals, G.L., Wasinger, V.C., Hochstrasser, D.F., and Sanchez, J.C. (2000) The dynamic range of protein expression: a challenge for proteomic research. Electrophoresis 21: 1104-1115.
    • (2000) Electrophoresis , vol.21 , pp. 1104-1115
    • Corthals, G.L.1    Wasinger, V.C.2    Hochstrasser, D.F.3    Sanchez, J.C.4
  • 49
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized ppb-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized ppb-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367-1372.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 50
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: matching proteins with mass spectra
    • Craig, R., and Beavis, R.C. (2004) TANDEM: matching proteins with mass spectra. Bioinformatics 20: 1466-1467.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 51
    • 21244443812 scopus 로고    scopus 로고
    • The use of proteotypic peptide libraries for protein identification
    • Craig, R., Cortens, J., and Beavis, R. (2005) The use of proteotypic peptide libraries for protein identification. Rapid Commun Mass Spectrom 19: 1844-1850.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 1844-1850
    • Craig, R.1    Cortens, J.2    Beavis, R.3
  • 52
    • 42349105213 scopus 로고    scopus 로고
    • Relative quantification of proteins in human cerebrospinal fluids by ms/ms using 6-plex isobaric tags
    • Dayon, L., Hainard, A., Licker, V., Turck, N., Kuhn, K., Hochstrasser, D.F., etal. (2008) Relative quantification of proteins in human cerebrospinal fluids by ms/ms using 6-plex isobaric tags. Anal Chem 80: 2921-2931.
    • (2008) Anal Chem , vol.80 , pp. 2921-2931
    • Dayon, L.1    Hainard, A.2    Licker, V.3    Turck, N.4    Kuhn, K.5    Hochstrasser, D.F.6
  • 53
    • 0033121118 scopus 로고    scopus 로고
    • Comparing protein profiles of 21 different activated sludge systems after SDS-PAGE
    • Ehler, M.M., and Cloete, T.E. (1999) Comparing protein profiles of 21 different activated sludge systems after SDS-PAGE. Water Res 33: 1181-1186.
    • (1999) Water Res , vol.33 , pp. 1181-1186
    • Ehler, M.M.1    Cloete, T.E.2
  • 54
    • 33750128393 scopus 로고    scopus 로고
    • The proteomic reactor: a microfluidic device for processing minute amounts of protein prior to mass spectrometry analysis
    • Eithier, M., Hou, W.M., Duewel, H.S., and Figeys, D. (2006) The proteomic reactor: a microfluidic device for processing minute amounts of protein prior to mass spectrometry analysis. J Proteome Res 5: 2754-2759.
    • (2006) J Proteome Res , vol.5 , pp. 2754-2759
    • Eithier, M.1    Hou, W.M.2    Duewel, H.S.3    Figeys, D.4
  • 55
    • 72449192318 scopus 로고    scopus 로고
    • Comparative study of the extracellular proteome of sulfolobus species reveals limited secretion
    • Ellen, A.F., Albers, S.V., and Driessen, A.J. (2009) Comparative study of the extracellular proteome of sulfolobus species reveals limited secretion. Extremophiles 14: 87-98.
    • (2009) Extremophiles , vol.14 , pp. 87-98
    • Ellen, A.F.1    Albers, S.V.2    Driessen, A.J.3
  • 56
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J.K., McCormack, A.L., and Yates, J.R., III (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
  • 57
    • 0036534547 scopus 로고    scopus 로고
    • Using stable-isotope-labeled proteins for hydrogen exchange studies in complex mixtures
    • Engen, J.R., Bradbury, E.M., and Chen, X. (2002) Using stable-isotope-labeled proteins for hydrogen exchange studies in complex mixtures. Anal Chem 74: 1680-1686.
    • (2002) Anal Chem , vol.74 , pp. 1680-1686
    • Engen, J.R.1    Bradbury, E.M.2    Chen, X.3
  • 59
    • 4043141477 scopus 로고    scopus 로고
    • Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research
    • Everley, P.A., Krijgsveld, J., Zetter, B.R., and Gygi, S.P. (2004) Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol Cell Proteomics 3: 729-735.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 729-735
    • Everley, P.A.1    Krijgsveld, J.2    Zetter, B.R.3    Gygi, S.P.4
  • 60
    • 34447570967 scopus 로고    scopus 로고
    • A review of quantitative methods for proteomic studies
    • Fenselau, C. (2007) A review of quantitative methods for proteomic studies. J Chromatogr B 855: 14-20.
    • (2007) J Chromatogr B , vol.855 , pp. 14-20
    • Fenselau, C.1
  • 61
    • 0033849339 scopus 로고    scopus 로고
    • Towards higher resolution: two-dimensional electrophoresis of Saccharomyces cerevisiae proteins using overlapping narrow immobilized pH gradients
    • Fey, S.J., Larsen, P.M., Görg, A., München, F., Weihenstephan, G., and Odense, D. (2000) Towards higher resolution: two-dimensional electrophoresis of Saccharomyces cerevisiae proteins using overlapping narrow immobilized pH gradients. Electrophoresis 21: 2610-2616.
    • (2000) Electrophoresis , vol.21 , pp. 2610-2616
    • Fey, S.J.1    Larsen, P.M.2    Görg, A.3    München, F.4    Weihenstephan, G.5    Odense, D.6
  • 62
    • 33847340190 scopus 로고    scopus 로고
    • Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ)
    • Gan, C.S., Chong, P.K., Pham, T.K., and Wright, P.C. (2007) Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ). J Proteome Res 6: 821-827.
    • (2007) J Proteome Res , vol.6 , pp. 821-827
    • Gan, C.S.1    Chong, P.K.2    Pham, T.K.3    Wright, P.C.4
  • 63
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S., Rush, J., Stemman, O., Kirschner, M., and Gygi, S. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 100: 6940-6945.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.1    Rush, J.2    Stemman, O.3    Kirschner, M.4    Gygi, S.5
  • 65
    • 2442679707 scopus 로고    scopus 로고
    • Proteomic analysis of an extreme halophilic archaeon, Halobacterium sp. NRC-1
    • Goo, Y.A., Yi, E.C., Baliga, N.S., Tao, W.A., Pan, M., Aebersold, R., etal. (2003) Proteomic analysis of an extreme halophilic archaeon, Halobacterium sp. NRC-1. Mol Cell Proteomics 2: 506-524.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 506-524
    • Goo, Y.A.1    Yi, E.C.2    Baliga, N.S.3    Tao, W.A.4    Pan, M.5    Aebersold, R.6
  • 66
    • 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, N.F., Guilhaus, M., and Cavicchioli, R. (2004a) 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.3    Guilhaus, M.4    Cavicchioli, R.5
  • 68
    • 17444384908 scopus 로고    scopus 로고
    • Cold adaptation of the Antarctic archaeon, Methanococcoides burtonii assessed by proteomics using ICAT
    • Goodchild, A., Raftery, M., Saunders, N.F., Guilhaus, M., and Cavicchioli, R. (2005) Cold adaptation of the Antarctic archaeon, Methanococcoides burtonii assessed by proteomics using ICAT. J Proteome Res 4: 473-480.
    • (2005) J Proteome Res , vol.4 , pp. 473-480
    • Goodchild, A.1    Raftery, M.2    Saunders, N.F.3    Guilhaus, M.4    Cavicchioli, R.5
  • 69
    • 0036731271 scopus 로고    scopus 로고
    • Proteomics without polyacrylamide: qualitative and quantitative uses of tandem mass spectrometry in proteome analysis
    • Goodlett, D.R., and Yi, E.C. (2002) Proteomics without polyacrylamide: qualitative and quantitative uses of tandem mass spectrometry in proteome analysis. Funct Integr Genomics 2: 138-153.
    • (2002) Funct Integr Genomics , vol.2 , pp. 138-153
    • Goodlett, D.R.1    Yi, E.C.2
  • 71
    • 33748304117 scopus 로고    scopus 로고
    • A combined shotgun and multidimensional proteomic analysis of the insoluble subproteome of the obligate thermophile, Geobacillus thermoleovorans t80
    • Graham, R.L., O'Loughlin, S.N., Pollock, C.E., Ternan, N.G., Weatherly, D.B., Jackson, P.J., etal. (2006a) A combined shotgun and multidimensional proteomic analysis of the insoluble subproteome of the obligate thermophile, Geobacillus thermoleovorans t80. J Proteome Res 5: 2465-2473.
    • (2006) J Proteome Res , vol.5 , pp. 2465-2473
    • Graham, R.L.1    O'Loughlin, S.N.2    Pollock, C.E.3    Ternan, N.G.4    Weatherly, D.B.5    Jackson, P.J.6
  • 72
    • 33645784124 scopus 로고    scopus 로고
    • Top-down proteomic analysis of the soluble sub-proteome of the obligate thermophile, Geobacillus thermoleovorans t80: insights into its cellular processes
    • Graham, R.L.J., Pollock, C.E., Ternan, N.G., and McMullan, G. (2006b) Top-down proteomic analysis of the soluble sub-proteome of the obligate thermophile, Geobacillus thermoleovorans t80: insights into its cellular processes. J Prot Res 5: 822-828.
    • (2006) J Prot Res , vol.5 , pp. 822-828
    • Graham, R.L.J.1    Pollock, C.E.2    Ternan, N.G.3    McMullan, G.4
  • 73
    • 33846640661 scopus 로고    scopus 로고
    • Multidimensional analysis of the insoluble sub-proteome of Oceanobacillus iheyensis hte831, an alkaliphilic and halotolerant deep-sea bacterium isolated from the Iheya Ridge
    • Graham, R.L., Pollock, C.E., O'Loughlin, S.N., Ternan, N.G., Weatherly, D.B., Tarleton, R.L., and McMullan, G. (2007) Multidimensional analysis of the insoluble sub-proteome of Oceanobacillus iheyensis hte831, an alkaliphilic and halotolerant deep-sea bacterium isolated from the Iheya Ridge. Proteomics 7: 82-91.
    • (2007) Proteomics , vol.7 , pp. 82-91
    • Graham, R.L.1    Pollock, C.E.2    O'Loughlin, S.N.3    Ternan, N.G.4    Weatherly, D.B.5    Tarleton, R.L.6    McMullan, G.7
  • 74
    • 42649132889 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5,111 proteins
    • Graumann, J., Hubner, N.C., Kim, J.B., Ko, K., Moser, M., Kumar, C., etal. (2008) Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5, 111 proteins. Mol Cell Proteomics 7: 672-683.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 672-683
    • Graumann, J.1    Hubner, N.C.2    Kim, J.B.3    Ko, K.4    Moser, M.5    Kumar, C.6
  • 75
    • 0035563654 scopus 로고    scopus 로고
    • Toward a high-throughput approach to quantitative proteomic analysis: expression-dependent protein identification by mass spectrometry
    • Griffin, T.J., Han, D.K., Gygi, S.P., Rist, B., Lee, H., Aebersold, R., and Parker, K.C. (2001) Toward a high-throughput approach to quantitative proteomic analysis: expression-dependent protein identification by mass spectrometry. J Am Soc Mass Spectrom 12: 1238-1246.
    • (2001) J Am Soc Mass Spectrom , vol.12 , pp. 1238-1246
    • Griffin, T.J.1    Han, D.K.2    Gygi, S.P.3    Rist, B.4    Lee, H.5    Aebersold, R.6    Parker, K.C.7
  • 76
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S.P., Rochon, Y., Franza, B.R., and Aebersold, R. (1999a) Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 19: 1720-1730.
    • (1999) Mol Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 77
    • 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., and Aebersold, R. (1999b) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17: 994-999.
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 78
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis based proteome analysis technology
    • Gygi, S.P., Corthals, G.L., Zhang, Y., Rochon, Y., and Aebersold, R. (2000) Evaluation of two-dimensional gel electrophoresis based proteome analysis technology. Proc Natl Acad Sci USA 97: 9390-9305.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9390-9305
    • Gygi, S.P.1    Corthals, G.L.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 79
    • 0036391454 scopus 로고    scopus 로고
    • Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinty tags
    • Gygi, S.P., Rist, B., Griffin, T.J., Eng, J.K., and Aebersold, R. (2002) Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinty tags. J Proteome Res 1: 47-54.
    • (2002) J Proteome Res , vol.1 , pp. 47-54
    • Gygi, S.P.1    Rist, B.2    Griffin, T.J.3    Eng, J.K.4    Aebersold, R.5
  • 82
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: a bridge between interactomics and structural biology
    • Heck, A.J.R. (2008) Native mass spectrometry: a bridge between interactomics and structural biology. Nat Methods 5: 927-933.
    • (2008) Nat Methods , vol.5 , pp. 927-933
    • Heck, A.J.R.1
  • 83
    • 33751340274 scopus 로고    scopus 로고
    • Comparison of spectral counting and metabolic stable isotope labeling for use with quantitative microbial proteomics
    • Hendrickson, E., Xia, Q., Wang, T., Leigh, J., and Hackett, M. (2006) Comparison of spectral counting and metabolic stable isotope labeling for use with quantitative microbial proteomics. Analyst 131: 1335-1341.
    • (2006) Analyst , vol.131 , pp. 1335-1341
    • Hendrickson, E.1    Xia, Q.2    Wang, T.3    Leigh, J.4    Hackett, M.5
  • 84
    • 0029670477 scopus 로고    scopus 로고
    • Translational control of p27KIP1 accumulation during the cell cycle
    • Hengst, L., and Reed, S.I. (1996) Translational control of p27KIP1 accumulation during the cell cycle. Science 271: 1861-1864.
    • (1996) Science , vol.271 , pp. 1861-1864
    • Hengst, L.1    Reed, S.I.2
  • 87
    • 16344384887 scopus 로고    scopus 로고
    • The importance of experimental design in proteomic mass spectrometry experiments: some cautionary tales
    • Hu, J., Coombes, K.R., Morris, J.S., and Baggerly, K.A. (2005a) The importance of experimental design in proteomic mass spectrometry experiments: some cautionary tales. Brief Funct Genomic Proteomic 3: 322-331.
    • (2005) Brief Funct Genomic Proteomic , vol.3 , pp. 322-331
    • Hu, J.1    Coombes, K.R.2    Morris, J.S.3    Baggerly, K.A.4
  • 89
    • 0000312004 scopus 로고
    • Protein sequencing by tandem mass spectrometry
    • Hunt, D.F., and Yates, J.R., III (1986) Protein sequencing by tandem mass spectrometry. Proc Acad Sci USA 83: 6233-6237.
    • (1986) Proc Acad Sci USA , vol.83 , pp. 6233-6237
    • Hunt, D.F.1    Yates III, J.R.2
  • 91
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (EMPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y., Oda, Y., Tabata, T., Sato, T., Nagasu, T., Rappsilber, J., and Mann, M. (2005) Exponentially modified protein abundance index (EMPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4: 1265-1272.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 92
    • 13144265766 scopus 로고    scopus 로고
    • Multidimensional separation of peptides for effective proteomic analysis
    • Issaq, H.J., Chan, K.C., Janini, G.M., Conrads, T.P., and Veenstra, T.D. (2005) Multidimensional separation of peptides for effective proteomic analysis. J Chromatogr B 817: 35-47.
    • (2005) J Chromatogr B , vol.817 , pp. 35-47
    • Issaq, H.J.1    Chan, K.C.2    Janini, G.M.3    Conrads, T.P.4    Veenstra, T.D.5
  • 94
    • 53049085850 scopus 로고    scopus 로고
    • Incorporation of carbon and nitrogen atoms into proteins measured by protein-based stable isotope probing (Protein-SIP)
    • Jemlich, N., Schmidt, F., Harwich, M., von Bergen, M., Richnow, H.-H., and Vogt, C. (2008) Incorporation of carbon and nitrogen atoms into proteins measured by protein-based stable isotope probing (Protein-SIP). Rapid Commun Mass Spectrom 22: 2889-2897.
    • (2008) Rapid Commun Mass Spectrom , vol.22 , pp. 2889-2897
    • Jemlich, N.1    Schmidt, F.2    Harwich, M.3    von Bergen, M.4    Richnow, H.-H.5    Vogt, C.6
  • 95
    • 67149131864 scopus 로고    scopus 로고
    • Comparison of methods for simultaneous identificatiopn of bacterial species and determination of metabolic activity by protein based stable isotope probing (Protein-SIP) experiments
    • Jemlich, N., Schmidt, F., Taubert, M., Seifert, J., von Bergen, M., Richnow, H.-H., and Vogt, C. (2009) Comparison of methods for simultaneous identificatiopn of bacterial species and determination of metabolic activity by protein based stable isotope probing (Protein-SIP) experiments. Rapid Commun Mass Spectrom 23: 1871-1878.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 1871-1878
    • Jemlich, N.1    Schmidt, F.2    Taubert, M.3    Seifert, J.4    von Bergen, M.5    Richnow, H.-H.6    Vogt, C.7
  • 97
    • 1642462855 scopus 로고    scopus 로고
    • 18O peptide ion ratios for the relative quantification of proteomes
    • 18O peptide ion ratios for the relative quantification of proteomes. J Am Soc Mass Spectrom 15: 437-445.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 437-445
    • Johnson, K.L.1    Muddiman, D.C.2
  • 98
    • 3543121341 scopus 로고    scopus 로고
    • Quantification in proteomics through stable isotope coding: a review
    • Julka, S., and Regnier, F. (2004) Quantification in proteomics through stable isotope coding: a review. J Proteome Res 3: 350-363.
    • (2004) J Proteome Res , vol.3 , pp. 350-363
    • Julka, S.1    Regnier, F.2
  • 99
    • 0037012884 scopus 로고    scopus 로고
    • Public-private group maps out initiatives
    • Kaiser, J. (2002) Public-private group maps out initiatives. Science 296: 827.
    • (2002) Science , vol.296 , pp. 827
    • Kaiser, J.1
  • 100
    • 33947600879 scopus 로고    scopus 로고
    • Metaproteomic analysis of Chesapeake Bay microbial communities
    • Kan, J., Hanson, T.E., Ginter, J.M., Wang, K., and Chen, F. (2005) Metaproteomic analysis of Chesapeake Bay microbial communities. Saline Systems 1: 1-7.
    • (2005) Saline Systems , vol.1 , pp. 1-7
    • Kan, J.1    Hanson, T.E.2    Ginter, J.M.3    Wang, K.4    Chen, F.5
  • 101
  • 102
    • 34548409217 scopus 로고    scopus 로고
    • Experimental and statistical considerations to avoid false conclusions in proteomic studies using differential in-gel electrophoresis
    • Karp, N.A., McCormick, P.S., Russell, M.R., and Lilley, K.S. (2007) Experimental and statistical considerations to avoid false conclusions in proteomic studies using differential in-gel electrophoresis. Mol Cell Proteomics 6: 1354-1364.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1354-1364
    • Karp, N.A.1    McCormick, P.S.2    Russell, M.R.3    Lilley, K.S.4
  • 104
    • 35748959321 scopus 로고    scopus 로고
    • Proteomic studies of an antarctic cold-adapted bacterium, Shewanella livingstonensis ac10, for global identification of cold-inducible proteins
    • Kawamoto, J., Kurihara, T., Kitagawa, M., Kato, I., and Esaki, N. (2007) Proteomic studies of an antarctic cold-adapted bacterium, Shewanella livingstonensis ac10, for global identification of cold-inducible proteins. Extremophiles 11: 819-826.
    • (2007) Extremophiles , vol.11 , pp. 819-826
    • Kawamoto, J.1    Kurihara, T.2    Kitagawa, M.3    Kato, I.4    Esaki, N.5
  • 105
    • 79952117670 scopus 로고    scopus 로고
    • Software pipeline and data analysis for ms/ms proteomics: the trans-proteomic pipeline
    • Keller, A., and Shteynberg, D. (2011) Software pipeline and data analysis for ms/ms proteomics: the trans-proteomic pipeline. Methods Mol Biol 694: 169-189.
    • (2011) Methods Mol Biol , vol.694 , pp. 169-189
    • Keller, A.1    Shteynberg, D.2
  • 106
    • 33746930864 scopus 로고    scopus 로고
    • A uniform proteomics MS/MS analysis platform utilizing open XML file formats
    • Keller, A., Eng, J., Zhang, N., Li, X., and Aebersold, R. (2005) A uniform proteomics MS/MS analysis platform utilizing open XML file formats. Mol Syst Biol 2: 1-8.
    • (2005) Mol Syst Biol , vol.2 , pp. 1-8
    • Keller, A.1    Eng, J.2    Zhang, N.3    Li, X.4    Aebersold, R.5
  • 107
    • 63849104493 scopus 로고    scopus 로고
    • Environmental proteomics: a paradigm shift in characterizing microbial activities at the molecular level
    • Keller, M., and Hettich, R. (2009) Environmental proteomics: a paradigm shift in characterizing microbial activities at the molecular level. Microbiol Mol Biol Rev 73: 62-70.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 62-70
    • Keller, M.1    Hettich, R.2
  • 108
    • 14044259281 scopus 로고    scopus 로고
    • Exploiting thiol modifications
    • Kiley, P.J., and Storz, G. (2004) Exploiting thiol modifications. PLoS Biol 2: e400.
    • (2004) PLoS Biol , vol.2
    • Kiley, P.J.1    Storz, G.2
  • 110
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick, D., Gerber, S., and Gygi, S. (2005) The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 35: 265-273.
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.1    Gerber, S.2    Gygi, S.3
  • 111
    • 33847177982 scopus 로고    scopus 로고
    • Metaproteomics approach to study the functionality of the microbiota in the human infant gastrointestional tract
    • Klaassens, E.S., de Vos, W.M., and Vaughan, E.E. (2007) Metaproteomics approach to study the functionality of the microbiota in the human infant gastrointestional tract. Appl Environ Microbiol 73: 1388-1392.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1388-1392
    • Klaassens, E.S.1    de Vos, W.M.2    Vaughan, E.E.3
  • 115
    • 15744384577 scopus 로고    scopus 로고
    • Quantitative proteomics by metabolic labeling with stable isotopes
    • Krijgsveld, J., and Heck, A.J.R. (2004) Quantitative proteomics by metabolic labeling with stable isotopes. Drug Discov Today: Targets 3: S11-S15.
    • (2004) Drug Discov Today: Targets , vol.3
    • Krijgsveld, J.1    Heck, A.J.R.2
  • 117
    • 79951896245 scopus 로고    scopus 로고
    • Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans
    • Kumsta, C., Thamsen, M., and Jakob, U. (2010) Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans. Antioxid Redox Signal 14: 1023-1037.
    • (2010) Antioxid Redox Signal , vol.14 , pp. 1023-1037
    • Kumsta, C.1    Thamsen, M.2    Jakob, U.3
  • 118
    • 61449182093 scopus 로고    scopus 로고
    • Proteomic characterization of the sulfur-reducing hyperthermophilic archaeon Thermococcus onnurineus na1 by 2-DE/MS-MS
    • Kwon, S.O., Kang, S.G., Park, S.H., Kim, Y.H., Choi, J.S., Lee, J., and Kim, S.I. (2009) Proteomic characterization of the sulfur-reducing hyperthermophilic archaeon Thermococcus onnurineus na1 by 2-DE/MS-MS. Extremophiles 13: 379-387.
    • (2009) Extremophiles , vol.13 , pp. 379-387
    • Kwon, S.O.1    Kang, S.G.2    Park, S.H.3    Kim, Y.H.4    Choi, J.S.5    Lee, J.6    Kim, S.I.7
  • 119
    • 63849227439 scopus 로고    scopus 로고
    • Environmental proteomics: applications of proteome profiling in environmental microbiology and biotechnology
    • Lacerda, C.M.R., and Reardon, K.F. (2009) Environmental proteomics: applications of proteome profiling in environmental microbiology and biotechnology. Brief Funct Genomic Proteomic 8: 75-87.
    • (2009) Brief Funct Genomic Proteomic , vol.8 , pp. 75-87
    • Lacerda, C.M.R.1    Reardon, K.F.2
  • 120
    • 33947577004 scopus 로고    scopus 로고
    • Metaproteomic analysis of bacterial community response to cadmium exposure
    • Lacerda, C.M.R., Choe, L.H., and Reardon, K.F. (2007) Metaproteomic analysis of bacterial community response to cadmium exposure. J Proteome Res 6: 1145-1152.
    • (2007) J Proteome Res , vol.6 , pp. 1145-1152
    • Lacerda, C.M.R.1    Choe, L.H.2    Reardon, K.F.3
  • 121
    • 0028176450 scopus 로고
    • The cellular concentration of the sigma s subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation, and protein stability
    • Lange, R., and Hengge-Aronis, R. (1994) The cellular concentration of the sigma s subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation, and protein stability. Gene Dev 8: 1600-1612.
    • (1994) Gene Dev , vol.8 , pp. 1600-1612
    • Lange, R.1    Hengge-Aronis, R.2
  • 122
    • 0037015610 scopus 로고    scopus 로고
    • Analysis of the Plasmodium falciparum proteome by high-accuracy mass spectrometry
    • Lasonder, E., Ishihama, Y., Andersen, J.S., Vermunt, A.M.W., Pain, A., Sauerwein, R.W., etal. (2002) Analysis of the Plasmodium falciparum proteome by high-accuracy mass spectrometry. Nature 419: 537-542.
    • (2002) Nature , vol.419 , pp. 537-542
    • Lasonder, E.1    Ishihama, Y.2    Andersen, J.S.3    Vermunt, A.M.W.4    Pain, A.5    Sauerwein, R.W.6
  • 123
    • 79955071958 scopus 로고    scopus 로고
    • An integrative study of a meromictic lake ecosystem in Antarctica
    • in press) doi:10.1038/ismej.2010.185.
    • Lauro, F.M., DeMaere, M.Z., Yau, S., Brown, M., Ng, C., Wilkins, D., etal. (2010) An integrative study of a meromictic lake ecosystem in Antarctica. ISME J (in press) doi:10.1038/ismej.2010.185.
    • (2010) ISME J
    • Lauro, F.M.1    DeMaere, M.Z.2    Yau, S.3    Brown, M.4    Ng, C.5    Wilkins, D.6
  • 124
    • 68549136910 scopus 로고    scopus 로고
    • Proteomics of Pyrococcus furiosus, a hyperthermophilic archaeon refractory to traditional methods
    • Lee, A.M., Sevinsky, J.R., Bundy, J.L., Grunden, A.M., and Stephenson, J.L., Jr (2009) Proteomics of Pyrococcus furiosus, a hyperthermophilic archaeon refractory to traditional methods. J Proteome Res 8: 3844-3851.
    • (2009) J Proteome Res , vol.8 , pp. 3844-3851
    • Lee, A.M.1    Sevinsky, J.R.2    Bundy, J.L.3    Grunden, A.M.4    Stephenson Jr, J.L.5
  • 125
    • 77952489390 scopus 로고    scopus 로고
    • Environmental metagenomics: an innovative resource for industrial biocatalysis
    • Lefevre, F., Jarrin, C., Ginolhac, A., Auriol, D., and Nalin, R. (2007) Environmental metagenomics: an innovative resource for industrial biocatalysis. Biocatal Biotransform 25: 242-250.
    • (2007) Biocatal Biotransform , vol.25 , pp. 242-250
    • Lefevre, F.1    Jarrin, C.2    Ginolhac, A.3    Auriol, D.4    Nalin, R.5
  • 127
    • 33645463331 scopus 로고    scopus 로고
    • MapQuant: open-source software for large-scale protein quantification
    • Leptos, K.C., Sarracino, D.A., Jaffe, J.D., Krastins, B., and Church, G.M. (2006) MapQuant: open-source software for large-scale protein quantification. Proteomics 6: 1770-1782.
    • (2006) Proteomics , vol.6 , pp. 1770-1782
    • Leptos, K.C.1    Sarracino, D.A.2    Jaffe, J.D.3    Krastins, B.4    Church, G.M.5
  • 128
    • 77953846853 scopus 로고    scopus 로고
    • Differential proteomic analysis using isotope-coded protein-labeling strategies: comparison, improvements and application to simulated microgravity effect on Cupriavidus metallidurans ch34
    • Leroy, B., Rosier, C., Erculisse, V., Leys, N., Mergeay, M., and Wattiez, R. (2010) Differential proteomic analysis using isotope-coded protein-labeling strategies: comparison, improvements and application to simulated microgravity effect on Cupriavidus metallidurans ch34. Proteomics 10: 2281-2291.
    • (2010) Proteomics , vol.10 , pp. 2281-2291
    • Leroy, B.1    Rosier, C.2    Erculisse, V.3    Leys, N.4    Mergeay, M.5    Wattiez, R.6
  • 129
    • 66749192040 scopus 로고    scopus 로고
    • Global protein level responses of Halobacterium salinarum NRC-1 to prolonged changes in external sodium chloride concentrations
    • Leuko, S., Raftery, M.J., Burns, B.P., Walter, M.R., and Neilan, B.A. (2009) Global protein level responses of Halobacterium salinarum NRC-1 to prolonged changes in external sodium chloride concentrations. J Proteome Res 8: 2218-2225.
    • (2009) J Proteome Res , vol.8 , pp. 2218-2225
    • Leuko, S.1    Raftery, M.J.2    Burns, B.P.3    Walter, M.R.4    Neilan, B.A.5
  • 130
    • 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., and Aebersold, R. (2003) Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry. Anal Chem 75: 6648-6657.
    • (2003) Anal Chem , vol.75 , pp. 6648-6657
    • Li, X.J.1    Zhang, H.2    Ranish, J.A.3    Aebersold, R.4
  • 131
    • 0041884952 scopus 로고    scopus 로고
    • Identification of 2D-gel proteins: a comparison of MALDI/TOF peptide mass mapping to μLC-ESI tandem mass spectrometry
    • Lim, H., Eng, J., Yates, J.R., III, Tollaksen, S., Giometti, C., Holden, J., etal. (2003) Identification of 2D-gel proteins: a comparison of MALDI/TOF peptide mass mapping to μLC-ESI tandem mass spectrometry. J Am Soc Mass Spectrom 14: 957.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 957
    • Lim, H.1    Eng, J.2    Yates III, J.R.3    Tollaksen, S.4    Giometti, C.5    Holden, J.6
  • 132
    • 33748327058 scopus 로고    scopus 로고
    • Multi-Q: a fully automated tool for multiplexed protein quantitation
    • Lin, W.T., Hung, W.N., Yian, Y.H., Wu, K.P., Han, C.L., Chen, Y.R., etal. (2006) Multi-Q: a fully automated tool for multiplexed protein quantitation. J Proteome Res 5: 2328-2338.
    • (2006) J Proteome Res , vol.5 , pp. 2328-2338
    • Lin, W.T.1    Hung, W.N.2    Yian, Y.H.3    Wu, K.P.4    Han, C.L.5    Chen, Y.R.6
  • 134
    • 0033667456 scopus 로고    scopus 로고
    • A comparison of silver stain and SYPRO ruby protein gel stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling
    • Lopez, M.F., Berggren, K., Chernokalskaya, E., Lazarev, A., Robinson, M., and Patton, W.F. (2000) A comparison of silver stain and SYPRO ruby protein gel stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling. Electrophoresis 21: 3673-3683.
    • (2000) Electrophoresis , vol.21 , pp. 3673-3683
    • Lopez, M.F.1    Berggren, K.2    Chernokalskaya, E.3    Lazarev, A.4    Robinson, M.5    Patton, W.F.6
  • 135
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expressionprofiling estimates the relative contributions of transcriptional and translational regulation
    • Lu, P., Vogel, C., Wang, R., Yao, X., and Marcotte, E.M. (2006) Absolute protein expressionprofiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25: 117-124.
    • (2006) Nat Biotechnol , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 136
    • 29244464778 scopus 로고    scopus 로고
    • Tube-gel digestion: a novel proteomic approach for high throughput analysis of membrane proteins
    • Lu, X., and Zhu, H. (2005) Tube-gel digestion: a novel proteomic approach for high throughput analysis of membrane proteins. Mol Cell Proteomics 4: 1948-1958.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1948-1958
    • Lu, X.1    Zhu, H.2
  • 138
    • 23044507211 scopus 로고    scopus 로고
    • Quantitative MS for proteomics: teaching a new dog old tricks
    • MacCoss, M.J., and Matthews, D.E. (2005) Quantitative MS for proteomics: teaching a new dog old tricks. Anal Chem 77: 294A-302A.
    • (2005) Anal Chem , vol.77
    • MacCoss, M.J.1    Matthews, D.E.2
  • 139
    • 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., and Yates, J.R., III (2003) A correlation algorithm for the automated quantitative analysis of shotgun proteomics data. Anal Chem 75: 6912-6921.
    • (2003) Anal Chem , vol.75 , pp. 6912-6921
    • MacCoss, M.J.1    Wu, C.C.2    Liu, H.3    Sadygov, R.4    Yates III, J.R.5
  • 140
    • 28544433959 scopus 로고    scopus 로고
    • Measurement of the isotope enrichment of stable isotope-labeled proteins using high-resolution mass spectra of peptides
    • MacCoss, M.J., Wu, C.C., Matthews, D.E., and Yates, J.R., III (2005) Measurement of the isotope enrichment of stable isotope-labeled proteins using high-resolution mass spectra of peptides. Anal Chem 77: 7646-7653.
    • (2005) Anal Chem , vol.77 , pp. 7646-7653
    • MacCoss, M.J.1    Wu, C.C.2    Matthews, D.E.3    Yates III, J.R.4
  • 141
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., and Jensen, O. (2003) Proteomic analysis of post-translational modifications. Nat Biotechnol 21: 255-261.
    • (2003) Nat Biotechnol , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.2
  • 142
    • 0344642960 scopus 로고    scopus 로고
    • Use of polyclonal antibodies to detect and quantify the NOR protein of nitriteoxidizers in complex environments
    • Maron, P.A., Coeur, C., Pink, C., Clays-Josserand, A., Lensi, R., Richaume, A., and Poetier, P. (2003) Use of polyclonal antibodies to detect and quantify the NOR protein of nitriteoxidizers in complex environments. J Microbiol Methods 53: 87-95.
    • (2003) J Microbiol Methods , vol.53 , pp. 87-95
    • Maron, P.A.1    Coeur, C.2    Pink, C.3    Clays-Josserand, A.4    Lensi, R.5    Richaume, A.6    Poetier, P.7
  • 143
    • 2642585515 scopus 로고    scopus 로고
    • Immunological method for direct assessment of the functionality of a denitrifying strain of Pseudomonas fluorescens in soil
    • Maron, P.A., Richaume, A., Poetier, P., Lata, J.C., and Lensi, R. (2004) Immunological method for direct assessment of the functionality of a denitrifying strain of Pseudomonas fluorescens in soil. J Microbiol Methods 53: 13-21.
    • (2004) J Microbiol Methods , vol.53 , pp. 13-21
    • Maron, P.A.1    Richaume, A.2    Poetier, P.3    Lata, J.C.4    Lensi, R.5
  • 144
    • 34248162330 scopus 로고    scopus 로고
    • Protein extraction and fingerprinting optimization of bacterial communities in natural Environment
    • Maron, P.A., Christophe, M., Severine, S., Houria, A., Philippe, L., and Lionel, R. (2006) Protein extraction and fingerprinting optimization of bacterial communities in natural Environment. Microb Ecol 53: 426-434.
    • (2006) Microb Ecol , vol.53 , pp. 426-434
    • Maron, P.A.1    Christophe, M.2    Severine, S.3    Houria, A.4    Philippe, L.5    Lionel, R.6
  • 145
    • 34248165412 scopus 로고    scopus 로고
    • Metaproteomics: a new approach for studying functional microbial ecology
    • Maron, P.A., Ranjard, L., Mougel, C., and Lemanceau, P. (2007) Metaproteomics: a new approach for studying functional microbial ecology. Microb Ecol 53: 486-493.
    • (2007) Microb Ecol , vol.53 , pp. 486-493
    • Maron, P.A.1    Ranjard, L.2    Mougel, C.3    Lemanceau, P.4
  • 146
    • 21244495253 scopus 로고    scopus 로고
    • The development of the DIGE system: 2D fluorescence difference gel analysis technology
    • Marouga, R., David, S., and 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
  • 147
    • 77956556817 scopus 로고    scopus 로고
    • Metaproteomic and metagenomic analyses of defined oceanic microbial populations using microwave cell fixation and flow cytometric sorting
    • Mary, I., Oliver, A., Skipp, P., Holland, R., Topping, J., Tarran, G., etal. (2010) Metaproteomic and metagenomic analyses of defined oceanic microbial populations using microwave cell fixation and flow cytometric sorting. FEMS Microbiol Ecol 74: 10-18.
    • (2010) FEMS Microbiol Ecol , vol.74 , pp. 10-18
    • Mary, I.1    Oliver, A.2    Skipp, P.3    Holland, R.4    Topping, J.5    Tarran, G.6
  • 148
    • 34547156610 scopus 로고    scopus 로고
    • A platform for accurate mass and time analyses of mass spectrometry data
    • May, D., Fitzgibbon, M., Liu, Y., Holzman, T., Eng, J., Kemp, C.J., etal. (2007) A platform for accurate mass and time analyses of mass spectrometry data. J Proteome Res 6: 2685-2694.
    • (2007) J Proteome Res , vol.6 , pp. 2685-2694
    • May, D.1    Fitzgibbon, M.2    Liu, Y.3    Holzman, T.4    Eng, J.5    Kemp, C.J.6
  • 149
    • 70349897069 scopus 로고    scopus 로고
    • The halophilic alkalithermophile Natranaerobius thermophilus adapts to multiple environmental extremes using a large repertoire of Na(K)/H antiporters
    • Mesbah, N.M., Cook, G.M., and Wiegel, J. (2009) The halophilic alkalithermophile Natranaerobius thermophilus adapts to multiple environmental extremes using a large repertoire of Na(K)/H antiporters. Mol Microbiol 74: 270-281.
    • (2009) Mol Microbiol , vol.74 , pp. 270-281
    • Mesbah, N.M.1    Cook, G.M.2    Wiegel, J.3
  • 150
    • 34249340772 scopus 로고    scopus 로고
    • Membrane proteomic analysis of Arabidopsis thalania using alternative solubilisation techniques
    • Mitra, S.K., Gantt, J.A., Ruby, J.F., Clouse, S.D., and Goshe, M.B. (2007) Membrane proteomic analysis of Arabidopsis thalania using alternative solubilisation techniques. J Proteome Res 6: 1933-1950.
    • (2007) J Proteome Res , vol.6 , pp. 1933-1950
    • Mitra, S.K.1    Gantt, J.A.2    Ruby, J.F.3    Clouse, S.D.4    Goshe, M.B.5
  • 151
    • 33846105280 scopus 로고    scopus 로고
    • 18O-labeling strategies for quantitative proteomics
    • 18O-labeling strategies for quantitative proteomics. Mass Spectrom Rev 26: 121-136.
    • (2007) Mass Spectrom Rev , vol.26 , pp. 121-136
    • Miyagi, M.1    Rao, K.C.2
  • 152
    • 29244488552 scopus 로고    scopus 로고
    • A hyperthermophilic laccase from Thermus thermophilus hb27
    • Miyazaki, K. (2005) A hyperthermophilic laccase from Thermus thermophilus hb27. Extremophiles 9: 415-425.
    • (2005) Extremophiles , vol.9 , pp. 415-425
    • Miyazaki, K.1
  • 154
    • 0142151385 scopus 로고    scopus 로고
    • Overcoming technical variation and biological variation in quantitative proteomics
    • Molloy, M.P., Brzezinsk, E.E., Hang, J., McDowell, M.T., and VanBogelen, R.A. (2003) Overcoming technical variation and biological variation in quantitative proteomics. Proteomics 3: 1912-1919.
    • (2003) Proteomics , vol.3 , pp. 1912-1919
    • Molloy, M.P.1    Brzezinsk, E.E.2    Hang, J.3    McDowell, M.T.4    VanBogelen, R.A.5
  • 155
    • 43249087428 scopus 로고    scopus 로고
    • Masic: a software program for fast quantitation and flexible visualization of chromatographic profiles from detected LC-MS(/MS) features
    • Monroe, M.E., Shaw, J.L., Daly, D.S., Adkins, J.N., and Smith, R.D. (2008) Masic: a software program for fast quantitation and flexible visualization of chromatographic profiles from detected LC-MS(/MS) features. Comput Biol Chem 32: 215-217.
    • (2008) Comput Biol Chem , vol.32 , pp. 215-217
    • Monroe, M.E.1    Shaw, J.L.2    Daly, D.S.3    Adkins, J.N.4    Smith, R.D.5
  • 156
    • 77951497989 scopus 로고    scopus 로고
    • Comparative metaproteomics reveals ocean-scale shifts in microbial nutrient utilization and energy transduction
    • Morris, R.M., Nunn, B.L., Frazar, C., Goodlett, D.R., Ting, Y.S., and Rocap, G. (2010) Comparative metaproteomics reveals ocean-scale shifts in microbial nutrient utilization and energy transduction. ISME J 4: 673-685.
    • (2010) ISME J , vol.4 , pp. 673-685
    • Morris, R.M.1    Nunn, B.L.2    Frazar, C.3    Goodlett, D.R.4    Ting, Y.S.5    Rocap, G.6
  • 158
    • 35848929694 scopus 로고    scopus 로고
    • Analysis and validation of proteomic data generated by tandem mass spectrometry
    • Nesvizhskii, A.I., Vitek, O., and Aebersold, R. (2007) Analysis and validation of proteomic data generated by tandem mass spectrometry. Nat Methods 4: 787-797.
    • (2007) Nat Methods , vol.4 , pp. 787-797
    • Nesvizhskii, A.I.1    Vitek, O.2    Aebersold, R.3
  • 159
    • 77954832678 scopus 로고    scopus 로고
    • Metaproteogenomic analysis of a dominant green sulfur bacterium of Ace Lake, Antarctica
    • Ng, C., DeMaere, M.Z., Williams, T.J., Lauro, F.M., Raftery, M., Gibson, J., etal. (2010) Metaproteogenomic analysis of a dominant green sulfur bacterium of Ace Lake, Antarctica. ISME J 4: 1002-1019.
    • (2010) ISME J , vol.4 , pp. 1002-1019
    • Ng, C.1    DeMaere, M.Z.2    Williams, T.J.3    Lauro, F.M.4    Raftery, M.5    Gibson, J.6
  • 160
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda, Y., Huang, K., Cross, F.R., Cowburn, D., and Chait, B.T. (1999) Accurate quantitation of protein expression and site-specific phosphorylation. Proc Natl Acad Sci U S A 96: 6591-6596.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 161
    • 0027178079 scopus 로고
    • Direct extraction of proteins from environmental samples
    • Ogunseitan, O.A. (1993) Direct extraction of proteins from environmental samples. J Microbiol Methods 17: 273-281.
    • (1993) J Microbiol Methods , vol.17 , pp. 273-281
    • Ogunseitan, O.A.1
  • 163
    • 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., and 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: 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , 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
  • 164
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S.E., Foster, L.J., and Mann, M. (2003a) Mass spectrometric-based approaches in quantitative proteomics. Methods 29: 124-130.
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 165
    • 0012351964 scopus 로고    scopus 로고
    • 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC)
    • 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC). J Proteome Res 2: 173-181.
    • (2003) J Proteome Res , vol.2 , pp. 173-181
    • Ong, S.E.1    Kratchmarova, I.2    Mann, M.3
  • 166
    • 77957202200 scopus 로고    scopus 로고
    • LTQ-iQuant: a freely available software pipeline for automated and accurate protein quantification of isobaric tagged peptide data from LTQ instruments
    • Onsongo, G., Stone, M.D., Van Riper, S.K., Chilton, J., Wu, B., Higgins, L., etal. (2010) LTQ-iQuant: a freely available software pipeline for automated and accurate protein quantification of isobaric tagged peptide data from LTQ instruments. Proteomics 10: 3533-3538.
    • (2010) Proteomics , vol.10 , pp. 3533-3538
    • Onsongo, G.1    Stone, M.D.2    Van Riper, S.K.3    Chilton, J.4    Wu, B.5    Higgins, L.6
  • 168
    • 70449412362 scopus 로고    scopus 로고
    • Itraq underestimation in simple and complex mixtures: 'The good, the bad and the ugly'
    • Ow, S.Y., Salim, M., Noirel, J., Evans, C., Rehman, I., and Wright, P.C. (2009) Itraq underestimation in simple and complex mixtures: 'The good, the bad and the ugly'. J Proteome Res 8: 5347-5355.
    • (2009) J Proteome Res , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 170
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey, A., and Mann, M. (2000) Proteomics to study genes and genomes. Nature 405: 837-846.
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 171
    • 34247642450 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of distinct mammalian mediator complexes using normalized spectral abundance factors
    • Paoletti, A.C., Parmely, T.J., Tomomori-Sato, C., Sato, S., Zhu, D., Conaway, R.C., etal. (2006) Quantitative proteomic analysis of distinct mammalian mediator complexes using normalized spectral abundance factors. Proc Natl Acad Sci USA 103: 18928-18933.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18928-18933
    • Paoletti, A.C.1    Parmely, T.J.2    Tomomori-Sato, C.3    Sato, S.4    Zhu, D.5    Conaway, R.C.6
  • 172
    • 71649085969 scopus 로고    scopus 로고
    • Evaluation of isotope-coded protein labeling (ICPL) in the quantitative analysis of complex proteomes
    • Paradela, A., Marcilla, M., Navajas, R., Ferreira, L., Ramos-Fernandez, A., Fernandez, M., etal. (2010) Evaluation of isotope-coded protein labeling (ICPL) in the quantitative analysis of complex proteomes. Talanta 80: 1496-1502.
    • (2010) Talanta , vol.80 , pp. 1496-1502
    • Paradela, A.1    Marcilla, M.2    Navajas, R.3    Ferreira, L.4    Ramos-Fernandez, A.5    Fernandez, M.6
  • 173
    • 41549117597 scopus 로고    scopus 로고
    • Aquantitative analysis software tool for mass spectrometry-based proteomics
    • Park, S.K., Venable, J.D., Xu, T., and Yates, J.R., III (2008) Aquantitative analysis software tool for mass spectrometry-based proteomics. Nat Methods 5: 319-322.
    • (2008) Nat Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates III, J.R.4
  • 174
    • 0042432365 scopus 로고    scopus 로고
    • High throughput proteome-wide precision measurements of protein expression using mass spectrometry
    • Pasa-Tolic, L., Jensen, P.K., Anderson, G.A., Lipton, M.S., Peden, K.K., Martinovic, S., etal. (1999) High throughput proteome-wide precision measurements of protein expression using mass spectrometry. J Am Chem Soc 121: 7949-7950.
    • (1999) J Am Chem Soc , vol.121 , pp. 7949-7950
    • Pasa-Tolic, L.1    Jensen, P.K.2    Anderson, G.A.3    Lipton, M.S.4    Peden, K.K.5    Martinovic, S.6
  • 175
    • 0028142375 scopus 로고
    • From electrophoretically separated protein to identification: strategies for sequence and mass analysis
    • Patterson, S.D. (1994) From electrophoretically separated protein to identification: strategies for sequence and mass analysis. Anal Biochem 221: 1-15.
    • (1994) Anal Biochem , vol.221 , pp. 1-15
    • Patterson, S.D.1
  • 176
    • 0034111635 scopus 로고    scopus 로고
    • A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics
    • Patton, W.F. (2000) A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics. Electrophoresis 21: 1123-1144.
    • (2000) Electrophoresis , vol.21 , pp. 1123-1144
    • Patton, W.F.1
  • 177
    • 0036669447 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis; better than a poke in the ICAT?
    • Patton, W.F., Schulenberg, B., and Steinberg, T.H. (2002) Two-dimensional gel electrophoresis; better than a poke in the ICAT? Curr Opin Biotechnol 13: 321-328.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 321-328
    • Patton, W.F.1    Schulenberg, B.2    Steinberg, T.H.3
  • 179
    • 0034757770 scopus 로고    scopus 로고
    • Proteomics: the move to mixtures
    • Peng, J., and Gygi, S.P. (2001) Proteomics: the move to mixtures. J Mass Spectrom 36: 1083-1091.
    • (2001) J Mass Spectrom , vol.36 , pp. 1083-1091
    • Peng, J.1    Gygi, S.P.2
  • 180
    • 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., and Cottrell, J.S. (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.2    Creasy, D.M.3    Cottrell, J.S.4
  • 181
    • 77955159809 scopus 로고    scopus 로고
    • Peptide labeling with isobaric tags yields higher identification rates using iTRAQ 4-plex compared to TMT 6-plex and iTRAQ 8-plex on LTQ orbitrap
    • Pichler, P., Kocher, T., Holzmann, J., Mazanek, M., Taus, T., Ammerer, G., and Mechtler, K. (2010) Peptide labeling with isobaric tags yields higher identification rates using iTRAQ 4-plex compared to TMT 6-plex and iTRAQ 8-plex on LTQ orbitrap. Anal Chem 82: 6549-6558.
    • (2010) Anal Chem , vol.82 , pp. 6549-6558
    • Pichler, P.1    Kocher, T.2    Holzmann, J.3    Mazanek, M.4    Taus, T.5    Ammerer, G.6    Mechtler, K.7
  • 182
    • 27844495651 scopus 로고    scopus 로고
    • Protein transport in archaea: sec and twin arginine translocation pathways
    • Pohlschroder, M., Gimenez, M.I., and Jarrell, K.F. (2005) Protein transport in archaea: sec and twin arginine translocation pathways. Curr Opin Microbiol 8: 713-719.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 713-719
    • Pohlschroder, M.1    Gimenez, M.I.2    Jarrell, K.F.3
  • 183
    • 33750201140 scopus 로고    scopus 로고
    • A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability
    • Prosinecki, V., Botelho, H.M., Francese, S., Mastrobuoni, G., Moneti, G., Urich, T., etal. (2006) A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability. J Proteome Res 5: 2720-2726.
    • (2006) J Proteome Res , vol.5 , pp. 2720-2726
    • Prosinecki, V.1    Botelho, H.M.2    Francese, S.3    Mastrobuoni, G.4    Moneti, G.5    Urich, T.6
  • 184
    • 34047216653 scopus 로고    scopus 로고
    • Directed evolution of tk-subtilisin from a hyperthermophilic archaeon: identification of a single amino acid substitution responsible for low-temperature adaptation
    • Pulido, M.A., Koga, Y., Takano, K., and Kanaya, S. (2007) Directed evolution of tk-subtilisin from a hyperthermophilic archaeon: identification of a single amino acid substitution responsible for low-temperature adaptation. Protein Eng Des Sel 20: 143-153.
    • (2007) Protein Eng Des Sel , vol.20 , pp. 143-153
    • Pulido, M.A.1    Koga, Y.2    Takano, K.3    Kanaya, S.4
  • 185
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains
    • Rabilloud, T. (2002) Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains. Proteomics 2: 3-10.
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 187
    • 43049103761 scopus 로고    scopus 로고
    • Selectivity of bacterial proteome fractionation based on differential solubility: a mass spectrometry evaluation
    • Ramos, Y., Garcia, Y., Llopiz, A., and Castellanos-Serra, L. (2008) Selectivity of bacterial proteome fractionation based on differential solubility: a mass spectrometry evaluation. Anal Biochem 377: 134-140.
    • (2008) Anal Biochem , vol.377 , pp. 134-140
    • Ramos, Y.1    Garcia, Y.2    Llopiz, A.3    Castellanos-Serra, L.4
  • 189
    • 0037224514 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber, J., Ryder, U., Lamond, A., and Mann, M. (2002) Large-scale proteomic analysis of the human spliceosome. Genome Res 12: 1231-1245.
    • (2002) Genome Res , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.3    Mann, M.4
  • 190
    • 13844276803 scopus 로고    scopus 로고
    • Prefractionation techniques in proteome analysis: the mining tools of the third millennium
    • Righetti, P.G., Castagna, A., Antonioli, P., and Boschetti, E. (2005) Prefractionation techniques in proteome analysis: the mining tools of the third millennium. Electrophoresis 26: 297-319.
    • (2005) Electrophoresis , vol.26 , pp. 297-319
    • Righetti, P.G.1    Castagna, A.2    Antonioli, P.3    Boschetti, E.4
  • 191
    • 9244226546 scopus 로고    scopus 로고
    • Design and analysis of experiments with high throughput biological assay data
    • Rocke, D.M. (2004) Design and analysis of experiments with high throughput biological assay data. Semin Cell Dev Biol 15: 703-713.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 703-713
    • Rocke, D.M.1
  • 192
    • 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., etal. (2004) Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 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
  • 193
    • 33748333118 scopus 로고    scopus 로고
    • Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the Antarctic archaeon Methanococcoides burtonii
    • Saunders, N.F., Ng, C., Raftery, M., Guilhaus, M., Goodchild, A., and Cavicchioli, R. (2006) Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the Antarctic archaeon Methanococcoides burtonii. J Proteome Res 5: 2457-2464.
    • (2006) J Proteome Res , vol.5 , pp. 2457-2464
    • Saunders, N.F.1    Ng, C.2    Raftery, M.3    Guilhaus, M.4    Goodchild, A.5    Cavicchioli, R.6
  • 195
    • 0037805644 scopus 로고    scopus 로고
    • Biotechnological prospects from metagenomics
    • Schloss, P.D., and Handelsman, J. (2003) Biotechnological prospects from metagenomics. Curr Opin Biotechnol 14: 303-310.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 303-310
    • Schloss, P.D.1    Handelsman, J.2
  • 196
    • 34250639490 scopus 로고    scopus 로고
    • Metagenomics, biotechnology with non-culturable microbes
    • Schmeisser, C., Steele, H., and Streit, W.R. (2007) Metagenomics, biotechnology with non-culturable microbes. Appl Microbiol Biotechnol 75: 955-962.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 955-962
    • Schmeisser, C.1    Steele, H.2    Streit, W.R.3
  • 197
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • Schmidt, A., Kellermann, J., and Lottspeich, F. (2005) 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
  • 198
    • 77149152780 scopus 로고    scopus 로고
    • Environmental proteomics: analysis of structure and function of microbial communities
    • Schneider, T., and Riedel, K. (2010) Environmental proteomics: analysis of structure and function of microbial communities. Proteomics 10: 785-798.
    • (2010) Proteomics , vol.10 , pp. 785-798
    • Schneider, T.1    Riedel, K.2
  • 199
    • 1642314524 scopus 로고    scopus 로고
    • A novel proteomic screen for peptide-protein interactions
    • Schulze, W.X., and Mann, M. (2004) A novel proteomic screen for peptide-protein interactions. J Biol Chem 279: 10756-10764.
    • (2004) J Biol Chem , vol.279 , pp. 10756-10764
    • Schulze, W.X.1    Mann, M.2
  • 200
    • 66149138814 scopus 로고    scopus 로고
    • De novo sequence analysis of N-terminal sulfonated peptides after in-gel guanidination
    • Sergeant, K., Beeumen, J.V., and Samyn, B. (2009) De novo sequence analysis of N-terminal sulfonated peptides after in-gel guanidination. Methods Mol Biol 519: 495-506.
    • (2009) Methods Mol Biol , vol.519 , pp. 495-506
    • Sergeant, K.1    Beeumen, J.V.2    Samyn, B.3
  • 202
    • 1242316198 scopus 로고    scopus 로고
    • Ultra-high-efficiency strong cation exchange LC/RPLC/MS/MS for high dynamic range characterization of the human plasma proteome
    • Shen, Y., Jacobs, J., Camp, D., 2nd, Fang, R., Moore, R., Smith, R., etal. (2004) Ultra-high-efficiency strong cation exchange LC/RPLC/MS/MS for high dynamic range characterization of the human plasma proteome. Anal Chem 76: 1134-1144.
    • (2004) Anal Chem , vol.76 , pp. 1134-1144
    • Shen, Y.1    Jacobs, J.2    Camp 2nd, D.3    Fang, R.4    Moore, R.5    Smith, R.6
  • 203
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterisation of proteins and proteomes
    • Shevchenko, A., Thomas, H., Havli, J., Olsen, J.V., and Mann, M. (2007) In-gel digestion for mass spectrometric characterisation of proteins and proteomes. Nat Protoc 1: 2856-2860.
    • (2007) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Thomas, H.2    Havli, J.3    Olsen, J.V.4    Mann, M.5
  • 204
    • 58149187662 scopus 로고    scopus 로고
    • Alkaline adaptation of proteins
    • In Siddiqui, K.S., and Thomas, T. (eds). New York: Nova biomedical books
    • Shirai, T., Kobayashi, T., Ito, S., and Horikoshi, K. (2008) Alkaline adaptation of proteins. In Protein Adaptation in Extremophiles. Siddiqui, K.S., and Thomas, T. (eds). New York: Nova biomedical books, pp. 105-141.
    • (2008) Protein Adaptation in Extremophiles , pp. 105-141
    • Shirai, T.1    Kobayashi, T.2    Ito, S.3    Horikoshi, K.4
  • 205
    • 84862243858 scopus 로고    scopus 로고
    • Siddiqui, K.S., and Thomas, T. (eds) Molecular anatomy and physiologyof proteins Uversky, V.N (series ed.) New York: Nova Biomedical Books.
    • Siddiqui, K.S., and Thomas, T. (eds) (2008) Protein Adaptation in Extremophiles. Molecular anatomy and physiologyof proteins Uversky, V.N (series ed.) New York: Nova Biomedical Books.
    • (2008) Protein Adaptation in Extremophiles
  • 206
    • 34248213322 scopus 로고    scopus 로고
    • The potential of soilprotein-based methods to indicate metal contamination
    • Singleton, I., Merringto, G., Colvan, S., and Delahunty, J.S. (2003) The potential of soilprotein-based methods to indicate metal contamination. Appl Soil Ecol 654: 1-8.
    • (2003) Appl Soil Ecol , vol.654 , pp. 1-8
    • Singleton, I.1    Merringto, G.2    Colvan, S.3    Delahunty, J.S.4
  • 207
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • Siuti, N., and Kelleher, N.L. (2007) Decoding protein modifications using top-down mass spectrometry. Nat Methods 4: 817-821.
    • (2007) Nat Methods , vol.4 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 209
    • 58049112263 scopus 로고    scopus 로고
    • Transport functions dominate the SAR11 metaproteome at low-nutrient extremes in the Sargasso Sea
    • Sowell, S.M., Wilhelm, L.J., Norbeck, A.D., Lipton, M.S., Nicora, C.D., Barofsky, D.F., etal. (2009) Transport functions dominate the SAR11 metaproteome at low-nutrient extremes in the Sargasso Sea. ISME J 3: 93-105.
    • (2009) ISME J , vol.3 , pp. 93-105
    • Sowell, S.M.1    Wilhelm, L.J.2    Norbeck, A.D.3    Lipton, M.S.4    Nicora, C.D.5    Barofsky, D.F.6
  • 210
    • 34548486688 scopus 로고    scopus 로고
    • Chip-based nano-LC-MS/MS identification of proteins in complex biological samples using a novel polymer microfluidic device
    • Srbek, J., Eickhoff, J., Effelsberg, U., Kraiczek, K., van de Goor, T., and Coufal, P. (2007) Chip-based nano-LC-MS/MS identification of proteins in complex biological samples using a novel polymer microfluidic device. J Sep Sci 30: 2046-2052.
    • (2007) J Sep Sci , vol.30 , pp. 2046-2052
    • Srbek, J.1    Eickhoff, J.2    Effelsberg, U.3    Kraiczek, K.4    van de Goor, T.5    Coufal, P.6
  • 211
    • 10644268451 scopus 로고    scopus 로고
    • Zooming in: fractionation strategies in proteomics
    • Stasyk, T., and Huber, L.A. (2004) Zooming in: fractionation strategies in proteomics. Proteomics 4: 3704-3716.
    • (2004) Proteomics , vol.4 , pp. 3704-3716
    • Stasyk, T.1    Huber, L.A.2
  • 213
    • 77956320089 scopus 로고    scopus 로고
    • Quantitative proteome and transcriptome analysis of the archaeon Thermoplasma acidophilum cultured under aerobic and anaerobic conditions
    • Sun, N., Pan, C., Nickell, S., Mann, M., Baumeister, W., and Nagy, I. (2010) Quantitative proteome and transcriptome analysis of the archaeon Thermoplasma acidophilum cultured under aerobic and anaerobic conditions. J Proteome Res 9: 4839-4850.
    • (2010) J Proteome Res , vol.9 , pp. 4839-4850
    • Sun, N.1    Pan, C.2    Nickell, S.3    Mann, M.4    Baumeister, W.5    Nagy, I.6
  • 214
    • 3042765151 scopus 로고    scopus 로고
    • Novel linear quadrupole ion trap/FT mass spectrometer: performance characterization and use in the comparative analysis of histone H3 post-translational modification
    • Syka, J.E., Marto, J.A., Bai, D.L., Horning, S., Senko, M.W., Schwartz, J.C., etal. (2004) Novel linear quadrupole ion trap/FT mass spectrometer: performance characterization and use in the comparative analysis of histone H3 post-translational modification. J Proteome Res 3: 621-626.
    • (2004) J Proteome Res , vol.3 , pp. 621-626
    • Syka, J.E.1    Marto, J.A.2    Bai, D.L.3    Horning, S.4    Senko, M.W.5    Schwartz, J.C.6
  • 215
    • 33747885134 scopus 로고    scopus 로고
    • A computational approach toward label-free protein quantification using predicted peptide detectability
    • Tang, H., Arnold, R., Alves, P., Xun, Z., Clemmer, D., Novotny, M., etal. (2006) A computational approach toward label-free protein quantification using predicted peptide detectability. Bioinformatics 22: e481-e488.
    • (2006) Bioinformatics , vol.22
    • Tang, H.1    Arnold, R.2    Alves, P.3    Xun, Z.4    Clemmer, D.5    Novotny, M.6
  • 216
    • 33847345976 scopus 로고    scopus 로고
    • Profiling the membrane proteome of Shewanella oneidensis mr-1 with new affinity labeling probes
    • Tang, X., Yi, W., Munske, G.R., Adhikari, D.P., Zakharova, N.L., and Bruce, J.E. (2007) Profiling the membrane proteome of Shewanella oneidensis mr-1 with new affinity labeling probes. J Proteome Res 6: 724-734.
    • (2007) J Proteome Res , vol.6 , pp. 724-734
    • Tang, X.1    Yi, W.2    Munske, G.R.3    Adhikari, D.P.4    Zakharova, N.L.5    Bruce, J.E.6
  • 217
    • 33748087472 scopus 로고    scopus 로고
    • The work of the human proteome organisation's proteomics standards initiative (HUPO PSI)
    • Taylor, C.F., Hermjakob, H., Julian, R.K., Jr, Garavelli, J.S., Aebersold, R., and Apweiler, R. (2006) The work of the human proteome organisation's proteomics standards initiative (HUPO PSI). OMICS 10: 145-151.
    • (2006) OMICS , vol.10 , pp. 145-151
    • Taylor, C.F.1    Hermjakob, H.2    Julian Jr, R.K.3    Garavelli, J.S.4    Aebersold, R.5    Apweiler, R.6
  • 220
    • 68549089164 scopus 로고    scopus 로고
    • Life-style changes of a halophilic archaeon analyzed by quantitative proteomics
    • Tebbe, A., Schmidt, A., Konstantinidis, K., Falb, M., Bisle, B., Klein, C., etal. (2009) Life-style changes of a halophilic archaeon analyzed by quantitative proteomics. Proteomics 9: 3843-3855.
    • (2009) Proteomics , vol.9 , pp. 3843-3855
    • Tebbe, A.1    Schmidt, A.2    Konstantinidis, K.3    Falb, M.4    Bisle, B.5    Klein, C.6
  • 221
    • 71049189969 scopus 로고    scopus 로고
    • Normalization and statistical analysis of quantitative proteomics data generated by metabolic labeling
    • Ting, L., Cowley, M.J., Hoon, S.L., Guilhaus, M., Raftery, M.J., and Cavicchioli, R. (2009) Normalization and statistical analysis of quantitative proteomics data generated by metabolic labeling. Mol Cell Proteomics 8: 2227-2242.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2227-2242
    • Ting, L.1    Cowley, M.J.2    Hoon, S.L.3    Guilhaus, M.4    Raftery, M.J.5    Cavicchioli, R.6
  • 222
  • 223
    • 44449127723 scopus 로고    scopus 로고
    • Correlating the transcriptome, proteome, and metabolome in the environmental adaptation of a hyperthermophile
    • Trauger, S.A., Kalisak, E., Kalisiak, J., Morita, H., Weinberg, M.V., Menon, A.L., etal. (2008) Correlating the transcriptome, proteome, and metabolome in the environmental adaptation of a hyperthermophile. J Proteome Res 7: 1027-1035.
    • (2008) J Proteome Res , vol.7 , pp. 1027-1035
    • Trauger, S.A.1    Kalisak, E.2    Kalisiak, J.3    Morita, H.4    Weinberg, M.V.5    Menon, A.L.6
  • 224
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: a single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M., and Minden, J. (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
    • Unlu, M.1    Morgan, M.2    Minden, J.3
  • 225
    • 38649098761 scopus 로고    scopus 로고
    • Characterization of global yeast quantitative proteome data generated from the wild-type and glucose repression Saccharomyces cerevisiae strains: the comparison of two quantitative methods
    • Usaite, R., Wohlschlegel, J., Venable, J.D., Park, S.K., Nielsen, J., Olsson, L., and Yates, J.R., III (2008) Characterization of global yeast quantitative proteome data generated from the wild-type and glucose repression Saccharomyces cerevisiae strains: the comparison of two quantitative methods. J Proteome Res 7: 266-275.
    • (2008) J Proteome Res , vol.7 , pp. 266-275
    • Usaite, R.1    Wohlschlegel, J.2    Venable, J.D.3    Park, S.K.4    Nielsen, J.5    Olsson, L.6    Yates III, J.R.7
  • 226
    • 76849109997 scopus 로고    scopus 로고
    • Size-sorting combined with improved nanocapillary liquid chromatography-mass spectrometry for identification of intact proteins up to 80kDa
    • Vellaichamy, A., Tran, J.C., Catherman, A.D., Lee, J.E., Kellie, J.F., Sweet, S.M.M., etal. (2010) Size-sorting combined with improved nanocapillary liquid chromatography-mass spectrometry for identification of intact proteins up to 80kDa. Anal Chem 82: 1234-1244.
    • (2010) Anal Chem , vol.82 , pp. 1234-1244
    • Vellaichamy, A.1    Tran, J.C.2    Catherman, A.D.3    Lee, J.E.4    Kellie, J.F.5    Sweet, S.M.M.6
  • 227
    • 14744293536 scopus 로고    scopus 로고
    • Automated approach for quantitative analysis of complex mixtures from tandem mass spectra
    • Venable, J.D., Dong, M.Q., Wohlschlegel, J., Dillin, A., and Yates, J.R., III (2004) Automated approach for quantitative analysis of complex 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
  • 228
    • 60749119754 scopus 로고    scopus 로고
    • Functional analysis of natural microbial consortia using community proteomics
    • VerBerkmoes, N.C., Denef, V.J., Hettich, R.L., and Banfield, J.F. (2009) Functional analysis of natural microbial consortia using community proteomics. Nat Rev Microbiol 7: 196-205.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 196-205
    • VerBerkmoes, N.C.1    Denef, V.J.2    Hettich, R.L.3    Banfield, J.F.4
  • 229
    • 20844461912 scopus 로고    scopus 로고
    • Intact-protein-based high resolution three dimensional quantitative analysis system for proteome profiling of biological fluids
    • Wang, H., Clouthier, S.G., Galchev, V., Misek, D.E., Duffner, U., Min, C.-K., etal. (2005) Intact-protein-based high resolution three dimensional quantitative analysis system for proteome profiling of biological fluids. Mol Cell Prot 4: 618-625.
    • (2005) Mol Cell Prot , vol.4 , pp. 618-625
    • Wang, H.1    Clouthier, S.G.2    Galchev, V.3    Misek, D.E.4    Duffner, U.5    Min, C.-K.6
  • 230
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang, W., Zhou, H., Lin, H., Roy, S., Shaler, T., Hill, L., etal. (2003) Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal Chem 75: 4818-4826.
    • (2003) Anal Chem , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3    Roy, S.4    Shaler, T.5    Hill, L.6
  • 231
    • 34548119185 scopus 로고    scopus 로고
    • A modified coomassie brilliant blue staining method at nanogram sensitivity compatible with proteomic analysis
    • Wang, X., Li, X., and Li, Y. (2007) A modified coomassie brilliant blue staining method at nanogram sensitivity compatible with proteomic analysis. Biotechnol Lett 29: 1599-1603.
    • (2007) Biotechnol Lett , vol.29 , pp. 1599-1603
    • Wang, X.1    Li, X.2    Li, Y.3
  • 232
    • 0035983403 scopus 로고    scopus 로고
    • 15N-metabolic labeling/mass spectrometry for comparative proteomics and rapid identification of protein markers/targets
    • 15N-metabolic labeling/mass spectrometry for comparative proteomics and rapid identification of protein markers/targets. Rapid Commun Mass Spectrom 16: 1389-1397.
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 1389-1397
    • Wang, Y.K.1    Ma, Z.2    Quinn, D.F.3    Fu, E.W.4
  • 233
    • 0034094451 scopus 로고    scopus 로고
    • Analysis of the microbial proteome
    • Washburn, M.P., and Yates, J.R. (2000) Analysis of the microbial proteome. Curr Opin Microbiol 3: 292-297.
    • (2000) Curr Opin Microbiol , vol.3 , pp. 292-297
    • Washburn, M.P.1    Yates, J.R.2
  • 234
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M.P., Wolters, D., and Yates, J.R., 3rd (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 3rd, J.R.3
  • 235
    • 0036535357 scopus 로고    scopus 로고
    • Analysis of quantitative proteomic data generated via multidimensional protein identification technology
    • Washburn, M.P., Ulaszek, R., Deciu, C., Schieltz, D.M., and Yates, J.R., III (2002a) Analysis of quantitative proteomic data generated via multidimensional protein identification technology. Anal Chem 74: 1650-1657.
    • (2002) Anal Chem , vol.74 , pp. 1650-1657
    • Washburn, M.P.1    Ulaszek, R.2    Deciu, C.3    Schieltz, D.M.4    Yates III, J.R.5
  • 236
    • 0036535357 scopus 로고    scopus 로고
    • Analysis of quantitative proteomic data generated via multidimensional protein identification technology
    • Washburn, M.P., Ulaszek, R., Deciu, C., Schieltz, D.M., and Yates, J.R., III (2002b) Analysis of quantitative proteomic data generated via multidimensional protein identification technology. Anal Chem 74: 1650-1657.
    • (2002) Anal Chem , vol.74 , pp. 1650-1657
    • Washburn, M.P.1    Ulaszek, R.2    Deciu, C.3    Schieltz, D.M.4    Yates III, J.R.5
  • 238
    • 33846071911 scopus 로고    scopus 로고
    • An integrated systems approach for understanding cellular responses to gamma radiation
    • Whitehead, K., Kish, A., Pan, M., Kaur, A., Reiss, D.J., King, N., etal. (2006) An integrated systems approach for understanding cellular responses to gamma radiation. Mol Syst Biol 2: 47.
    • (2006) Mol Syst Biol , vol.2 , pp. 47
    • Whitehead, K.1    Kish, A.2    Pan, M.3    Kaur, A.4    Reiss, D.J.5    King, N.6
  • 239
    • 13344269000 scopus 로고    scopus 로고
    • From proteins to proteomes: large scale protein identification by two-dimensional electrophoresis and amino acid analysis
    • Wilkins, M.R., Pasquali, C., Appel, R.D., Ou, K., Golaz, O., Sanchez, J., etal. (1996) From proteins to proteomes: large scale protein identification by two-dimensional electrophoresis and amino acid analysis. Bio/Technology 14: 61-65.
    • (1996) Bio/Technology , vol.14 , pp. 61-65
    • Wilkins, M.R.1    Pasquali, C.2    Appel, R.D.3    Ou, K.4    Golaz, O.5    Sanchez, J.6
  • 241
    • 76149128021 scopus 로고    scopus 로고
    • Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part ii: the effect of different methylated growth substrates
    • Williams, T.J., Burg, D.W., Ertan, H., Raftery, M.J., Poljak, A., Guilhaus, M., and Cavicchioli, R. (2010a) Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part ii: the effect of different methylated growth substrates. J Proteome Res 9: 653-663.
    • (2010) J Proteome Res , vol.9 , pp. 653-663
    • Williams, T.J.1    Burg, D.W.2    Ertan, H.3    Raftery, M.J.4    Poljak, A.5    Guilhaus, M.6    Cavicchioli, R.7
  • 242
    • 76149124222 scopus 로고    scopus 로고
    • Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part i: the effect of growth temperature
    • Williams, T.J., Burg, D.W., Raftery, M.J., Poljak, A., Guilhaus, M., Pilak, O., and Cavicchioli, R. (2010b) Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part i: the effect of growth temperature. J Proteome Res 9: 640-652.
    • (2010) J Proteome Res , vol.9 , pp. 640-652
    • Williams, T.J.1    Burg, D.W.2    Raftery, M.J.3    Poljak, A.4    Guilhaus, M.5    Pilak, O.6    Cavicchioli, R.7
  • 244
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., and Mann, M. (1996) Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379: 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 245
    • 4344646435 scopus 로고    scopus 로고
    • The application of two-dimensional polyacrylamide gel electrophoresis and downstream analyses to a mixed community of prokaryotic microorganisms
    • Wilmes, P., and Bond, P.L. (2004) The application of two-dimensional polyacrylamide gel electrophoresis and downstream analyses to a mixed community of prokaryotic microorganisms. Environ Microbiol 6: 911-920.
    • (2004) Environ Microbiol , vol.6 , pp. 911-920
    • Wilmes, P.1    Bond, P.L.2
  • 246
    • 31944437874 scopus 로고    scopus 로고
    • Metaprotemics: studying functional gene expression in microbial ecosystems
    • Wilmes, P., and Bond, P.L. (2006) Metaprotemics: studying functional gene expression in microbial ecosystems. Trends Microbiol 14: 92-97.
    • (2006) Trends Microbiol , vol.14 , pp. 92-97
    • Wilmes, P.1    Bond, P.L.2
  • 247
    • 1542509482 scopus 로고    scopus 로고
    • Differential polypeptide display: the search for the elusive target
    • Wittke, S., Kaiser, T., and Mischak, H. (2004) Differential polypeptide display: the search for the elusive target. J Chromatogr B 803: 17-26.
    • (2004) J Chromatogr B , vol.803 , pp. 17-26
    • Wittke, S.1    Kaiser, T.2    Mischak, H.3
  • 248
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C.C., MacCoss, M.J., Howell, K.E., and Yates, J.R., 3rd (2003) A method for the comprehensive proteomic analysis of membrane proteins. Nat Biotechnol 21: 532-538.
    • (2003) Nat Biotechnol , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates 3rd, J.R.4
  • 249
    • 33646927488 scopus 로고    scopus 로고
    • Quantitative proteomics of the archaeon Methanococcus maripaludis validated by microarray analysis and real time PCR
    • Xia, Q., Hendrickson, E.L., Zhang, Y., Wang, T., Taub, F., Moore, B.C., etal. (2006) Quantitative proteomics of the archaeon Methanococcus maripaludis validated by microarray analysis and real time PCR. Mol Cell Proteomics 5: 868-881.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 868-881
    • Xia, Q.1    Hendrickson, E.L.2    Zhang, Y.3    Wang, T.4    Taub, F.5    Moore, B.C.6
  • 250
    • 33750620682 scopus 로고    scopus 로고
    • Differential quantitative proteomics of Porphyromonas gingivalis by linear ion trap mass spectrometry: non-label methods comparison, q-values and lowess curve fitting
    • Xia, Q., Wang, T., Park, Y., Lamont, R.J., and Hackett, M. (2007) Differential quantitative proteomics of Porphyromonas gingivalis by linear ion trap mass spectrometry: non-label methods comparison, q-values and lowess curve fitting. Int J Mass Spectrom 259: 105-116.
    • (2007) Int J Mass Spectrom , vol.259 , pp. 105-116
    • Xia, Q.1    Wang, T.2    Park, Y.3    Lamont, R.J.4    Hackett, M.5
  • 251
    • 19444363756 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomic profiling
    • Yan, W., and Chen, S.S. (2005) Mass spectrometry-based quantitative proteomic profiling. Brief Funct Genomic Proteomic 4: 1-12.
    • (2005) Brief Funct Genomic Proteomic , vol.4 , pp. 1-12
    • Yan, W.1    Chen, S.S.2
  • 253
    • 3042689578 scopus 로고    scopus 로고
    • Mass spectral analysis in proteomics
    • Yates, J.R., III (2004) Mass spectral analysis in proteomics. Annu Rev Bioph Biom 33: 297-316.
    • (2004) Annu Rev Bioph Biom , vol.33 , pp. 297-316
    • Yates III, J.R.1
  • 255
    • 0033972697 scopus 로고    scopus 로고
    • Separation of peptides by strong cation-exchange capillary electrochromatography
    • Ye, M., Zou, H., Liu, Z., and Ni, J. (2000) Separation of peptides by strong cation-exchange capillary electrochromatography. J Chromatogr A 869: 385-394.
    • (2000) J Chromatogr A , vol.869 , pp. 385-394
    • Ye, M.1    Zou, H.2    Liu, Z.3    Ni, J.4
  • 256
    • 72449170468 scopus 로고    scopus 로고
    • 'Hot standards' For the thermoacidophilic archaeon Sulfolobus solfataricus
    • Zaparty, M., Esser, D., Gertig, S., Haferkamp, P., Kouril, T., Manica, A., etal. (2010) 'Hot standards' For the thermoacidophilic archaeon Sulfolobus solfataricus. Extremophiles 14: 119-142.
    • (2010) Extremophiles , vol.14 , pp. 119-142
    • Zaparty, M.1    Esser, D.2    Gertig, S.3    Haferkamp, P.4    Kouril, T.5    Manica, A.6
  • 258
    • 33847681015 scopus 로고    scopus 로고
    • Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for escherichia coli membrane proteome analysis by 2-D LC-MS/MS
    • Zhang, N., Chen, R., Young, N., Wishart, D., Winter, P., Weiner, J.H., and Li, L. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7: 484-493.
    • (2007) Proteomics , vol.7 , pp. 484-493
    • Zhang, N.1    Chen, R.2    Young, N.3    Wishart, D.4    Winter, P.5    Weiner, J.H.6    Li, L.7
  • 259
    • 36048982541 scopus 로고    scopus 로고
    • Membrane subproteomic analysis of Mycobacterium bovis bacillus calmette-guerin
    • Zheng, J., Wei, C., Leng, W., Dong, J., Li, R., Li, W., etal. (2007) Membrane subproteomic analysis of Mycobacterium bovis bacillus calmette-guerin. Proteomics 7: 3919-3931.
    • (2007) Proteomics , vol.7 , pp. 3919-3931
    • Zheng, J.1    Wei, C.2    Leng, W.3    Dong, J.4    Li, R.5    Li, W.6
  • 260
    • 11144333521 scopus 로고    scopus 로고
    • 15N-labeled and unlabeled peptides for efficient protein identification and de novo peptide sequencing
    • 15N-labeled and unlabeled peptides for efficient protein identification and de novo peptide sequencing. J Proteome Res 3: 1155-1163.
    • (2004) J Proteome Res , vol.3 , pp. 1155-1163
    • Zhong, H.1    Marcus, S.L.2    Li, L.3
  • 261
    • 4444282445 scopus 로고    scopus 로고
    • Shotgun proteomics of Methanococcus jannaschii and insights into methanogenesis
    • Zhu, W., Reich, C.I., Olsen, G.J., Giometti, C.S., and Yates, J.R., 3rd (2004) Shotgun proteomics of Methanococcus jannaschii and insights into methanogenesis. J Proteome Res 3: 538-548.
    • (2004) J Proteome Res , vol.3 , pp. 538-548
    • Zhu, W.1    Reich, C.I.2    Olsen, G.J.3    Giometti, C.S.4    Yates 3rd, J.R.5
  • 262
    • 33646269941 scopus 로고    scopus 로고
    • TM reagent technology for protein complex and profiling studies
    • TM reagent technology for protein complex and profiling studies. J Exp Bot 57: 1501-1508.
    • (2006) J Exp Bot , vol.57 , pp. 1501-1508
    • Zieske, L.1
  • 263
    • 67650763466 scopus 로고    scopus 로고
    • Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the archaea
    • Zivanovic, Y., Armengaud, J., Lagorce, A., Leplat, C., Guerin, P., etal. (2009) Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the archaea. Genome Biol 10: R70.
    • (2009) Genome Biol , vol.10
    • Zivanovic, Y.1    Armengaud, J.2    Lagorce, A.3    Leplat, C.4    Guerin, P.5
  • 264
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • Zybailov, B., Coleman, M.K., Florens, L., and Washburn, M.P. (2005) Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling. Anal Chem 77: 6218-6224.
    • (2005) Anal Chem , vol.77 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.K.2    Florens, L.3    Washburn, M.P.4
  • 265
    • 33748319353 scopus 로고    scopus 로고
    • Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae
    • Zybailov, B., Mosley, A.L., Sardiu, M.E., Coleman, M.K., Florens, L., and Washburn, M.P. (2006) Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae. J Proteome Res 5: 2339-2347.
    • (2006) J Proteome Res , vol.5 , pp. 2339-2347
    • Zybailov, B.1    Mosley, A.L.2    Sardiu, M.E.3    Coleman, M.K.4    Florens, L.5    Washburn, M.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.