메뉴 건너뛰기




Volumn 72, Issue 5, 2009, Pages 771-784

Label-free quantitative proteomics of two Bifidobacterium longum strains

Author keywords

Bifidobacteria; DeCyder MS; Heat shock tolerance; Label free quantification

Indexed keywords

BACTERIAL PROTEIN;

EID: 67649503203     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2009.03.004     Document Type: Article
Times cited : (22)

References (64)
  • 1
    • 0036710314 scopus 로고    scopus 로고
    • Probiotics as modulators of the gut flora
    • Fooks L.J., and Gibson G.R. Probiotics as modulators of the gut flora. Br J Nutr 88 Suppl 1 (2002) S39-S49
    • (2002) Br J Nutr , vol.88 , Issue.SUPPL. 1
    • Fooks, L.J.1    Gibson, G.R.2
  • 2
    • 0033950802 scopus 로고    scopus 로고
    • Survival and therapeutic potential of probiotic organisms with reference to Lactobacillus acidophilus and Bifidobacterium spp
    • Kailasapathy K., and Chin J. Survival and therapeutic potential of probiotic organisms with reference to Lactobacillus acidophilus and Bifidobacterium spp. Immunol Cell Biol 78 (2000) 80-88
    • (2000) Immunol Cell Biol , vol.78 , pp. 80-88
    • Kailasapathy, K.1    Chin, J.2
  • 3
    • 0142122636 scopus 로고    scopus 로고
    • Immunomodulatory effects of probiotic bacteria DNA: IL-1 and IL-10 response in human peripheral blood mononuclear cells
    • Lammers K.M., Brigidi P., Vitali B., Gionchetti P., Rizzello F., Caramelli E., et al. Immunomodulatory effects of probiotic bacteria DNA: IL-1 and IL-10 response in human peripheral blood mononuclear cells. FEMS Immunol Med Microbiol 38 (2003) 165-172
    • (2003) FEMS Immunol Med Microbiol , vol.38 , pp. 165-172
    • Lammers, K.M.1    Brigidi, P.2    Vitali, B.3    Gionchetti, P.4    Rizzello, F.5    Caramelli, E.6
  • 4
    • 3142536964 scopus 로고    scopus 로고
    • Human studies on probiotics: what is scientifically proven
    • Salminen S., and Gueimonde M. Human studies on probiotics: what is scientifically proven. J Food Sci 69 (2004) M137-M140
    • (2004) J Food Sci , vol.69
    • Salminen, S.1    Gueimonde, M.2
  • 5
    • 18844388947 scopus 로고    scopus 로고
    • A proteomic view of Bifidobacterium infantis generated by multi-dimensional chromatography coupled with tandem mass spectrometry
    • Vitali B., Wasinger V., Brigidi P., and Guilhaus M. A proteomic view of Bifidobacterium infantis generated by multi-dimensional chromatography coupled with tandem mass spectrometry. Proteomics 5 (2005) 1859-1867
    • (2005) Proteomics , vol.5 , pp. 1859-1867
    • Vitali, B.1    Wasinger, V.2    Brigidi, P.3    Guilhaus, M.4
  • 6
    • 33745587005 scopus 로고    scopus 로고
    • A proteome reference map and proteomic analysis of Bifidobacterium longum NCC2705
    • Yuan J., Zhu L., Liu X., Li T., Zhang Y., Ying T., et al. A proteome reference map and proteomic analysis of Bifidobacterium longum NCC2705. Mol. Cell Proteomics 5 (2006) 1105-1118
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1105-1118
    • Yuan, J.1    Zhu, L.2    Liu, X.3    Li, T.4    Zhang, Y.5    Ying, T.6
  • 7
    • 38649114046 scopus 로고    scopus 로고
    • Analysis of host-inducing proteome changes in Bifidobacterium longum NCC2705 grown in vivo
    • Yuan J., Wang B., Sun Z., Bo X., Yuan X., He X., et al. Analysis of host-inducing proteome changes in Bifidobacterium longum NCC2705 grown in vivo. J Proteome Res 7 (2008) 375-385
    • (2008) J Proteome Res , vol.7 , pp. 375-385
    • Yuan, J.1    Wang, B.2    Sun, Z.3    Bo, X.4    Yuan, X.5    He, X.6
  • 9
    • 0034630225 scopus 로고    scopus 로고
    • Basic features of the stress response in three species of bifidobacteria: B. longum, B. adolescentis, and B. breve
    • Schmidt G., and Zink R. Basic features of the stress response in three species of bifidobacteria: B. longum, B. adolescentis, and B. breve. Int J Food Microbiol 55 (2000) 41-45
    • (2000) Int J Food Microbiol , vol.55 , pp. 41-45
    • Schmidt, G.1    Zink, R.2
  • 10
    • 8144219531 scopus 로고    scopus 로고
    • Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003: genetic, transcriptional, and phylogenetic analyses
    • Ventura M., Canchaya C., Zink R., Fitzgerald G.F., and van Sinderen D. Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003: genetic, transcriptional, and phylogenetic analyses. Appl Environ Microbiol 70 (2004) 6197-6209
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6197-6209
    • Ventura, M.1    Canchaya, C.2    Zink, R.3    Fitzgerald, G.F.4    van Sinderen, D.5
  • 11
    • 12244311206 scopus 로고    scopus 로고
    • Gene structure and transcriptional organization of the dnaK operon of Bifidobacterium breve UCC 2003 and application of the operon in bifidobacterial tracing
    • Ventura M., Zink R., Fitzgerald G.F., and van Sinderen D. Gene structure and transcriptional organization of the dnaK operon of Bifidobacterium breve UCC 2003 and application of the operon in bifidobacterial tracing. Appl Environ Microbiol 71 (2005) 487-500
    • (2005) Appl Environ Microbiol , vol.71 , pp. 487-500
    • Ventura, M.1    Zink, R.2    Fitzgerald, G.F.3    van Sinderen, D.4
  • 12
    • 24944547568 scopus 로고    scopus 로고
    • The clpB gene of Bifidobacterium breve UCC 2003: transcriptional analysis and first insights into stress induction
    • Ventura M., Kenny J.G., Zhang Z., Fitzgerald G.F., and van Sinderen D. The clpB gene of Bifidobacterium breve UCC 2003: transcriptional analysis and first insights into stress induction. Microbiology 151 (2005) 2861-2872
    • (2005) Microbiology , vol.151 , pp. 2861-2872
    • Ventura, M.1    Kenny, J.G.2    Zhang, Z.3    Fitzgerald, G.F.4    van Sinderen, D.5
  • 14
    • 3242776249 scopus 로고    scopus 로고
    • Rapid identification of stress-related fingerprint from whole bacterial cells of Bifidobacterium lactis using matrix assisted laser desorption/ionization mass spectrometry
    • Marvin-Guy L.F., Parche S., Wagniere S., Moulin J., Zink R., Kussmann M., et al. Rapid identification of stress-related fingerprint from whole bacterial cells of Bifidobacterium lactis using matrix assisted laser desorption/ionization mass spectrometry. J Am Soc Mass Spectrom 15 (2004) 1222-1227
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 1222-1227
    • Marvin-Guy, L.F.1    Parche, S.2    Wagniere, S.3    Moulin, J.4    Zink, R.5    Kussmann, M.6
  • 15
    • 21744455549 scopus 로고    scopus 로고
    • Effect of heat-shock and bile salts on protein synthesis of Bifidobacterium longum revealed by [35S]methionine labelling and two-dimensional gel electrophoresis
    • Savijoki K., Suokko A., Palva A., Valmu L., Kalkkinen N., and Varmanen P. Effect of heat-shock and bile salts on protein synthesis of Bifidobacterium longum revealed by [35S]methionine labelling and two-dimensional gel electrophoresis. FEMS Microbiol Lett 248 (2005) 207-215
    • (2005) FEMS Microbiol Lett , vol.248 , pp. 207-215
    • Savijoki, K.1    Suokko, A.2    Palva, A.3    Valmu, L.4    Kalkkinen, N.5    Varmanen, P.6
  • 16
    • 23644445359 scopus 로고    scopus 로고
    • Proteomic analysis of global changes in protein expression during bile salt exposure of Bifidobacterium longum NCIMB 8809
    • Sanchez B., Champomier-Verges M.C., Anglade P., Baraige F., de Los Reyes-Gavilan C.G., Margolles A., et al. Proteomic analysis of global changes in protein expression during bile salt exposure of Bifidobacterium longum NCIMB 8809. J Bacteriol 187 (2005) 5799-5808
    • (2005) J Bacteriol , vol.187 , pp. 5799-5808
    • Sanchez, B.1    Champomier-Verges, M.C.2    Anglade, P.3    Baraige, F.4    de Los Reyes-Gavilan, C.G.5    Margolles, A.6
  • 17
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg A., Weiss W., and Dunn M.J. Current two-dimensional electrophoresis technology for proteomics. Proteomics 4 (2004) 3665-3685
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 18
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data
    • Nesvizhskii A.I., and Aebersold R. Interpretation of shotgun proteomic data. Mol Cell Proteomics 4 (2005) 1419-1440
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 19
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters D.A., Washburn M.P., and Yates J.R. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem 73 (2001) 5683-5690
    • (2001) Anal Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates, J.R.3
  • 20
    • 3543121341 scopus 로고    scopus 로고
    • Quantification in proteomics through stable isotope coding: a review
    • Julka S., and Regnier F. Quantification in proteomics through stable isotope coding: a review. J Proteome Res 3 (2004) 350-363
    • (2004) J Proteome Res , vol.3 , pp. 350-363
    • Julka, S.1    Regnier, F.2
  • 21
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H.B., Sadygov R.G., and Yates III J.R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76 (2004) 4193-4201
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.B.1    Sadygov, R.G.2    Yates III, J.R.3
  • 23
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • Mueller L.N., Brusniak M.Y., Mani D.R., and Aebersold R. An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. J Proteome Res 7 (2008) 51-61
    • (2008) J Proteome Res , vol.7 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.Y.2    Mani, D.R.3    Aebersold, R.4
  • 24
    • 40549107755 scopus 로고    scopus 로고
    • Comparative LC-MS: a landscape of peaks and valleys
    • America A.H., and Cordewener J.H. Comparative LC-MS: a landscape of peaks and valleys. Proteomics 8 (2008) 731-749
    • (2008) Proteomics , vol.8 , pp. 731-749
    • America, A.H.1    Cordewener, J.H.2
  • 25
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M. Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 7 (2006) 952-958
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 26
    • 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. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17 (1999) 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
  • 27
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross P.L., Huang Y.N., Marchese J.N., Williamson B., Parker K., Hattan S., et al. Multiplexed protein quantitation in saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 3 (2004) 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
  • 28
    • 32044443141 scopus 로고    scopus 로고
    • Two-dimensional mass spectrometric mapping
    • Roesli C., Elia G., and Neri D. Two-dimensional mass spectrometric mapping. Curr Opin Chem Biol 10 (2006) 35-41
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 35-41
    • Roesli, C.1    Elia, G.2    Neri, D.3
  • 29
    • 17844394177 scopus 로고    scopus 로고
    • Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry
    • Listgarten J., and Emili A. Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics 4 (2005) 419-434
    • (2005) Mol Cell Proteomics , vol.4 , pp. 419-434
    • Listgarten, J.1    Emili, A.2
  • 30
    • 33646264529 scopus 로고    scopus 로고
    • Advances in proteomics data analysis and display using an accurate mass and time tag approach
    • Zimmer J.S., Monroe M.E., Qian W.J., and Smith R.D. Advances in proteomics data analysis and display using an accurate mass and time tag approach. Mass Spectrom Rev 25 (2006) 450-482
    • (2006) Mass Spectrom Rev , vol.25 , pp. 450-482
    • Zimmer, J.S.1    Monroe, M.E.2    Qian, W.J.3    Smith, R.D.4
  • 31
    • 33645725976 scopus 로고    scopus 로고
    • Simultaneous qualitative and quantitative analysis of the Escherichia coli proteome: a sweet tale
    • Silva J.C., Denny R., Dorschel C., Gorenstein M.V., Li G.Z., Richardson K., et al. Simultaneous qualitative and quantitative analysis of the Escherichia coli proteome: a sweet tale. Mol Cell Proteomics 5 (2006) 589-607
    • (2006) Mol Cell Proteomics , vol.5 , pp. 589-607
    • Silva, J.C.1    Denny, R.2    Dorschel, C.3    Gorenstein, M.V.4    Li, G.Z.5    Richardson, K.6
  • 32
    • 33748376902 scopus 로고    scopus 로고
    • Differential expression analysis of Escherichia coli proteins using a novel software for relative quantitation of LC-MS/MS data
    • Johansson C., Samskog J., Sundstrom L., Wadensten H., Bjorkesten L., and Flensburg J. Differential expression analysis of Escherichia coli proteins using a novel software for relative quantitation of LC-MS/MS data. Proteomics 6 (2006) 4475-4485
    • (2006) Proteomics , vol.6 , pp. 4475-4485
    • Johansson, C.1    Samskog, J.2    Sundstrom, L.3    Wadensten, H.4    Bjorkesten, L.5    Flensburg, J.6
  • 33
    • 0037195083 scopus 로고    scopus 로고
    • The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract
    • Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., et al. The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract. Proc Natl Acad Sci U.S.A 99 (2002) 14422-14427
    • (2002) Proc Natl Acad Sci U.S.A , vol.99 , pp. 14422-14427
    • Schell, M.A.1    Karmirantzou, M.2    Snel, B.3    Vilanova, D.4    Berger, B.5    Pessi, G.6
  • 34
    • 67649525729 scopus 로고    scopus 로고
    • Natural selection and molecular characterization of Bifidobacterium longum heat-shock tolerant mutants
    • submitted
    • Berger B, Moine D, Mansourian R, Arigoni F. Natural selection and molecular characterization of Bifidobacterium longum heat-shock tolerant mutants. submitted.
    • Berger, B.1    Moine, D.2    Mansourian, R.3    Arigoni, F.4
  • 35
    • 18844388947 scopus 로고    scopus 로고
    • A proteomic view of Bifidobacterium infantis generated by multi-dimensional chromatography coupled with tandem mass spectrometry
    • Vitali B., Wasinger V., Brigidi P., and Guilhaus M. A proteomic view of Bifidobacterium infantis generated by multi-dimensional chromatography coupled with tandem mass spectrometry. Proteomics 5 (2005) 1859-1867
    • (2005) Proteomics , vol.5 , pp. 1859-1867
    • Vitali, B.1    Wasinger, V.2    Brigidi, P.3    Guilhaus, M.4
  • 36
    • 8344284323 scopus 로고    scopus 로고
    • A common open representation of mass spectrometry data and its application to proteomics research
    • Pedrioli P.G., Eng J.K., Hubley R., Vogelzang M., Deutsch E.W., Raught B., et al. A common open representation of mass spectrometry data and its application to proteomics research. Nat. Biotechnol 22 (2004) 1459-1466
    • (2004) Nat. Biotechnol , vol.22 , pp. 1459-1466
    • Pedrioli, P.G.1    Eng, J.K.2    Hubley, R.3    Vogelzang, M.4    Deutsch, E.W.5    Raught, B.6
  • 37
    • 33646564676 scopus 로고    scopus 로고
    • Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes
    • Wang G., Wu W.W., Zeng W., Chou C.L., and Shen R.F. Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes. J. Proteome. Res 5 (2006) 1214-1223
    • (2006) J. Proteome. Res , vol.5 , pp. 1214-1223
    • Wang, G.1    Wu, W.W.2    Zeng, W.3    Chou, C.L.4    Shen, R.F.5
  • 38
    • 33748376902 scopus 로고    scopus 로고
    • Differential expression analysis of Escherichia coli proteins using a novel software for relative quantitation of LC-MS/MS data
    • Johansson C., Samskog J., Sundstrom L., Wadensten H., Bjorkesten L., and Flensburg J. Differential expression analysis of Escherichia coli proteins using a novel software for relative quantitation of LC-MS/MS data. Proteomics 6 (2006) 4475-4485
    • (2006) Proteomics , vol.6 , pp. 4475-4485
    • Johansson, C.1    Samskog, J.2    Sundstrom, L.3    Wadensten, H.4    Bjorkesten, L.5    Flensburg, J.6
  • 39
    • 18844388947 scopus 로고    scopus 로고
    • A proteomic view of Bifidobacterium infantis generated by multi-dimensional chromatography coupled with tandem mass spectrometry
    • Vitali B., Wasinger V., Brigidi P., and Guilhaus M. A proteomic view of Bifidobacterium infantis generated by multi-dimensional chromatography coupled with tandem mass spectrometry. Proteomics 5 (2005) 1859-1867
    • (2005) Proteomics , vol.5 , pp. 1859-1867
    • Vitali, B.1    Wasinger, V.2    Brigidi, P.3    Guilhaus, M.4
  • 40
    • 33745587005 scopus 로고    scopus 로고
    • A proteome reference map and proteomic analysis of Bifidobacterium longum NCC2705
    • Yuan J., Zhu L., Liu X., Li T., Zhang Y., Ying T., et al. A proteome reference map and proteomic analysis of Bifidobacterium longum NCC2705. Mol Cell Proteomics 5 (2006) 1105-1118
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1105-1118
    • Yuan, J.1    Zhu, L.2    Liu, X.3    Li, T.4    Zhang, Y.5    Ying, T.6
  • 41
    • 0037307837 scopus 로고    scopus 로고
    • Stable isotope-coded proteomic mass spectrometry
    • Goshe M.B., and Smith R.D. Stable isotope-coded proteomic mass spectrometry. Curr Opin Biotechnol 14 (2003) 101-109
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 101-109
    • Goshe, M.B.1    Smith, R.D.2
  • 42
    • 42649098635 scopus 로고    scopus 로고
    • ANIBAL-stable-isotope-based quantitative proteomics by ANIline and Benzoic acid labeling of amino and carboxylic groups
    • Panchaud A., Hansson J., Affolter M., Rhlid R.B., Piu S., Moreillon P., et al. ANIBAL-stable-isotope-based quantitative proteomics by ANIline and Benzoic acid labeling of amino and carboxylic groups. Mol Cell Proteomics 7 (2008) 800-812
    • (2008) Mol Cell Proteomics , vol.7 , pp. 800-812
    • Panchaud, A.1    Hansson, J.2    Affolter, M.3    Rhlid, R.B.4    Piu, S.5    Moreillon, P.6
  • 45
    • 23944470664 scopus 로고    scopus 로고
    • Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display
    • Tammen H., Schulte I., Hess R., Menzel C., Kellmann M., Mohring T., et al. Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics 5 (2005) 3414-3422
    • (2005) Proteomics , vol.5 , pp. 3414-3422
    • Tammen, H.1    Schulte, I.2    Hess, R.3    Menzel, C.4    Kellmann, M.5    Mohring, T.6
  • 46
    • 3042739098 scopus 로고    scopus 로고
    • A tool to visualize and evaluate data obtained by liquid chromatography-electrospray ionization-mass spectrometry
    • Li X.J., Pedrioli P.G., Eng J., Martin D., Yi E.C., Lee H., et al. A tool to visualize and evaluate data obtained by liquid chromatography-electrospray ionization-mass spectrometry. Anal Chem 76 (2004) 3856-3860
    • (2004) Anal Chem , vol.76 , pp. 3856-3860
    • Li, X.J.1    Pedrioli, P.G.2    Eng, J.3    Martin, D.4    Yi, E.C.5    Lee, H.6
  • 48
    • 25444526868 scopus 로고    scopus 로고
    • Processing methods for differential analysis of LC/MS profile data
    • Katajamaa M., and Oresic M. Processing methods for differential analysis of LC/MS profile data. BMC Bioinformatics 6 (2005) 179
    • (2005) BMC Bioinformatics , vol.6 , pp. 179
    • Katajamaa, M.1    Oresic, M.2
  • 49
  • 50
    • 26844492976 scopus 로고    scopus 로고
    • A software suite for the generation and comparison of peptide arrays from sets of data collected by liquid chromatography-mass spectrometry
    • Li X.J., Yi E.C., Kemp C.J., Zhang H., and Aebersold R. A software suite for the generation and comparison of peptide arrays from sets of data collected by liquid chromatography-mass spectrometry. Mol Cell Proteom 4 (Sep 2005) 1328 1340
    • (2005) Mol Cell Proteom , vol.4
    • Li, X.J.1    Yi, E.C.2    Kemp, C.J.3    Zhang, H.4    Aebersold, R.5
  • 51
    • 33747180294 scopus 로고    scopus 로고
    • A suite of algorithms for the comprehensive analysis of complex protein mixtures using high-resolution LC-MS
    • Bellew M., Coram M., Fitzgibbon M., Igra M., Randolph T., Wang P., et al. A suite of algorithms for the comprehensive analysis of complex protein mixtures using high-resolution LC-MS. Bioinformatics 22 (2006) 1902-1909
    • (2006) Bioinformatics , vol.22 , pp. 1902-1909
    • Bellew, M.1    Coram, M.2    Fitzgibbon, M.3    Igra, M.4    Randolph, T.5    Wang, P.6
  • 53
    • 10744228656 scopus 로고    scopus 로고
    • Determination of peptides and proteins in human urine with capillary electrophoresis-mass spectrometry, a suitable tool for the establishment of new diagnostic markers
    • Wittke S., Fliser D., Haubitz M., Bartel S., Krebs R., Hausadel F., et al. Determination of peptides and proteins in human urine with capillary electrophoresis-mass spectrometry, a suitable tool for the establishment of new diagnostic markers. J Chromatogr A 1013 (2003) 173-181
    • (2003) J Chromatogr A , vol.1013 , pp. 173-181
    • Wittke, S.1    Fliser, D.2    Haubitz, M.3    Bartel, S.4    Krebs, R.5    Hausadel, F.6
  • 54
    • 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.A., Hill L.R., et al. Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal Chem 75 (2003) 4818-4826
    • (2003) Anal Chem , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3    Roy, S.4    Shaler, T.A.5    Hill, L.R.6
  • 56
    • 14344250874 scopus 로고    scopus 로고
    • Informatics platform for global proteomic profiling and biomarker discovery using liquid chromatography-tandem mass spectrometry
    • Radulovic D., Jelveh S., Ryu S., Hamilton T.G., Foss E., Mao Y., et al. Informatics platform for global proteomic profiling and biomarker discovery using liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics 3 (2004) 984-997
    • (2004) Mol Cell Proteomics , vol.3 , pp. 984-997
    • Radulovic, D.1    Jelveh, S.2    Ryu, S.3    Hamilton, T.G.4    Foss, E.5    Mao, Y.6
  • 57
    • 34248176336 scopus 로고    scopus 로고
    • Discovering robust protein biomarkers for disease from relative expression reversals in 2-D DIGE data
    • Anderson T.J., Tchernyshyov I., Diez R., Cole R.N., Geman D., Dang C.V., et al. Discovering robust protein biomarkers for disease from relative expression reversals in 2-D DIGE data. Proteomics 7 (2007) 1197-1207
    • (2007) Proteomics , vol.7 , pp. 1197-1207
    • Anderson, T.J.1    Tchernyshyov, I.2    Diez, R.3    Cole, R.N.4    Geman, D.5    Dang, C.V.6
  • 58
    • 33748376902 scopus 로고    scopus 로고
    • Differential expression analysis of Escherichia coli proteins using a novel software for relative quantitation of LC-MS/MS data
    • Johansson C., Samskog J., Sundstrom L., Wadensten H., Bjorkesten L., and Flensburg J. Differential expression analysis of Escherichia coli proteins using a novel software for relative quantitation of LC-MS/MS data. Proteomics 6 (2006) 4475-4485
    • (2006) Proteomics , vol.6 , pp. 4475-4485
    • Johansson, C.1    Samskog, J.2    Sundstrom, L.3    Wadensten, H.4    Bjorkesten, L.5    Flensburg, J.6
  • 59
    • 8144219531 scopus 로고    scopus 로고
    • Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003: genetic, transcriptional, and phylogenetic analyses
    • Ventura M., Canchaya C., Zink R., Fitzgerald G.F., and van Sinderen D. Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003: genetic, transcriptional, and phylogenetic analyses. Appl Environ Microbiol 70 (2004) 6197-6209
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6197-6209
    • Ventura, M.1    Canchaya, C.2    Zink, R.3    Fitzgerald, G.F.4    van Sinderen, D.5
  • 60
    • 0029161644 scopus 로고
    • The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock protein which binds to the promoter region of the operon
    • Bucca G., Ferina G., Puglia A.M., and Smith C.P. The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock protein which binds to the promoter region of the operon. Mol Microbiol 17 (1995) 663-674
    • (1995) Mol Microbiol , vol.17 , pp. 663-674
    • Bucca, G.1    Ferina, G.2    Puglia, A.M.3    Smith, C.P.4
  • 61
    • 0030883870 scopus 로고    scopus 로고
    • Regulation of the dnaK operon of Streptomyces coelicolor A3(2) is governed by HspR, an autoregulatory repressor protein
    • Bucca G., Hindle Z., and Smith C.P. Regulation of the dnaK operon of Streptomyces coelicolor A3(2) is governed by HspR, an autoregulatory repressor protein. J Bacteriol 179 (1997) 5999-6004
    • (1997) J Bacteriol , vol.179 , pp. 5999-6004
    • Bucca, G.1    Hindle, Z.2    Smith, C.P.3
  • 62
    • 0031022299 scopus 로고    scopus 로고
    • Disruption of hspR, the repressor gene of the dnaK operon in Streptomyces albus G
    • Grandvalet C., Servant P., and Mazodier P. Disruption of hspR, the repressor gene of the dnaK operon in Streptomyces albus G. Mol Microbiol 23 (1997) 77-84
    • (1997) Mol Microbiol , vol.23 , pp. 77-84
    • Grandvalet, C.1    Servant, P.2    Mazodier, P.3
  • 63
    • 0034530509 scopus 로고    scopus 로고
    • The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co-repressordagger
    • Bucca G., Brassington A.M., Schonfeld H.J., and Smith C.P. The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co-repressordagger. Mol Microbiol 38 (2000) 1093-1103
    • (2000) Mol Microbiol , vol.38 , pp. 1093-1103
    • Bucca, G.1    Brassington, A.M.2    Schonfeld, H.J.3    Smith, C.P.4
  • 64
    • 0141818925 scopus 로고    scopus 로고
    • Negative feedback regulation of dnaK, clpB and lon expression by the DnaK chaperone machine in Streptomyces coelicolor, identified by transcriptome and in vivo DnaK-depletion analysis
    • Bucca G., Brassington A.M., Hotchkiss G., Mersinias V., and Smith C.P. Negative feedback regulation of dnaK, clpB and lon expression by the DnaK chaperone machine in Streptomyces coelicolor, identified by transcriptome and in vivo DnaK-depletion analysis. Mol Microbiol 50 (2003) 153-166
    • (2003) Mol Microbiol , vol.50 , pp. 153-166
    • Bucca, G.1    Brassington, A.M.2    Hotchkiss, G.3    Mersinias, V.4    Smith, C.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.