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Volumn 83, Issue , 2013, Pages 99-118

Charting the cellular and extracellular proteome analysis of Brevibacterium linens DSM 20158 with unsequenced genome by mass spectrometry-driven sequence similarity searches

Author keywords

Actinobacteria; B. linens; Cellular proteome; De novo sequencing; Extracellular proteome; NLC MS MS

Indexed keywords

CELL PROTEIN;

EID: 84876463512     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.02.029     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0033125574 scopus 로고    scopus 로고
    • Aspects of enzymology and biochemical properties of Brevibacterium linens relevant to cheese ripening: a review
    • Rattray F.P., Fox P.F. Aspects of enzymology and biochemical properties of Brevibacterium linens relevant to cheese ripening: a review. J Dairy Sci 1999, 82:891-909.
    • (1999) J Dairy Sci , vol.82 , pp. 891-909
    • Rattray, F.P.1    Fox, P.F.2
  • 2
    • 20544457348 scopus 로고    scopus 로고
    • Industrial importance of the genus Brevibacterium
    • Onraedt A., Soetaert W., Vandamme E. Industrial importance of the genus Brevibacterium. Biotechnol Lett 2005, 27:527-533.
    • (2005) Biotechnol Lett , vol.27 , pp. 527-533
    • Onraedt, A.1    Soetaert, W.2    Vandamme, E.3
  • 3
    • 0036263746 scopus 로고    scopus 로고
    • Intraspecific diversity of Brevibacterium linens, Corynebacterium glutamicum and Rhodococcus erythropolis based on partial 16S rDNA sequence analysis and Fourier-transform infrared (FT-IR) spectroscopy
    • Oberreuter H., Charzinski J., Scherer S. Intraspecific diversity of Brevibacterium linens, Corynebacterium glutamicum and Rhodococcus erythropolis based on partial 16S rDNA sequence analysis and Fourier-transform infrared (FT-IR) spectroscopy. Microbiology 2002, 148:1523-1532.
    • (2002) Microbiology , vol.148 , pp. 1523-1532
    • Oberreuter, H.1    Charzinski, J.2    Scherer, S.3
  • 4
    • 0042431982 scopus 로고    scopus 로고
    • The respiratory chain of Corynebacterium glutamicum
    • Bott M., Niebisch A. The respiratory chain of Corynebacterium glutamicum. J Biotechnol 2003, 104:129-153.
    • (2003) J Biotechnol , vol.104 , pp. 129-153
    • Bott, M.1    Niebisch, A.2
  • 5
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B., Aebersold R. Mass spectrometry and protein analysis. Science 2006, 312:212-217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 6
    • 77951022016 scopus 로고    scopus 로고
    • A comparison of the accuracy of iTRAQ quantification by nLC-ESI MSMS and nLC-MALDI MSMS methods
    • Shirran S.L., Botting C.H. A comparison of the accuracy of iTRAQ quantification by nLC-ESI MSMS and nLC-MALDI MSMS methods. J Proteomics 2010, 73:1391-1403.
    • (2010) J Proteomics , vol.73 , pp. 1391-1403
    • Shirran, S.L.1    Botting, C.H.2
  • 7
    • 55749101543 scopus 로고    scopus 로고
    • From complementarity to comprehensiveness-targeting the membrane proteome of growing Bacillus subtilis by divergent approaches
    • Hahne H., Wolff S., Hecker M., Becher D. From complementarity to comprehensiveness-targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 2008, 8:4123-4136.
    • (2008) Proteomics , vol.8 , pp. 4123-4136
    • Hahne, H.1    Wolff, S.2    Hecker, M.3    Becher, D.4
  • 8
    • 65449164977 scopus 로고    scopus 로고
    • LC-MS/MS-based proteome profiling in Daphnia pulex and Daphnia longicephala: the Daphnia pulex genome database as a key for high throughput proteomics in Daphnia
    • Frohlich T., Arnold G.J., Fritsch R., Mayr T., Laforsch C. LC-MS/MS-based proteome profiling in Daphnia pulex and Daphnia longicephala: the Daphnia pulex genome database as a key for high throughput proteomics in Daphnia. BMC Genomics 2009, 10:171.
    • (2009) BMC Genomics , vol.10 , pp. 171
    • Frohlich, T.1    Arnold, G.J.2    Fritsch, R.3    Mayr, T.4    Laforsch, C.5
  • 9
    • 46549085508 scopus 로고    scopus 로고
    • Assessment of protoxin composition of Bacillus thuringiensis strains by use of polyacrylamide gel block and mass spectrometry
    • Fu Z., Sun Y., Xia L., Ding X., Mo X., Li X., et al. Assessment of protoxin composition of Bacillus thuringiensis strains by use of polyacrylamide gel block and mass spectrometry. Appl Microbiol Biotechnol 2008, 79:875-880.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 875-880
    • Fu, Z.1    Sun, Y.2    Xia, L.3    Ding, X.4    Mo, X.5    Li, X.6
  • 11
    • 0022321245 scopus 로고
    • Determination of Sepharose-bound protein with Coomassie brilliant blue G-250
    • Asryants R.A., Duszenkova I.V., Nagradova N.K. Determination of Sepharose-bound protein with Coomassie brilliant blue G-250. Anal Biochem 1985, 151:571-574.
    • (1985) Anal Biochem , vol.151 , pp. 571-574
    • Asryants, R.A.1    Duszenkova, I.V.2    Nagradova, N.K.3
  • 12
    • 33646550516 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Escherichia coli W3110
    • Nandakumar M.P., Cheung A., Marten M.R. Proteomic analysis of extracellular proteins from Escherichia coli W3110. J Proteome Res 2006, 5:1155-1161.
    • (2006) J Proteome Res , vol.5 , pp. 1155-1161
    • Nandakumar, M.P.1    Cheung, A.2    Marten, M.R.3
  • 13
    • 33847035852 scopus 로고    scopus 로고
    • Isolation and identification of alpha-amylase producing Bacillus sp. from dhal industry waste
    • Thippeswamy S., Girigowda K., Mulimani V.H. Isolation and identification of alpha-amylase producing Bacillus sp. from dhal industry waste. Indian J Biochem Biophys 2006, 43:295-298.
    • (2006) Indian J Biochem Biophys , vol.43 , pp. 295-298
    • Thippeswamy, S.1    Girigowda, K.2    Mulimani, V.H.3
  • 14
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 1996, 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 15
    • 84863510942 scopus 로고    scopus 로고
    • Exploration of respiratory chain of Nocardia asteroides: purification of succinate quinone oxidoreductase
    • Ahmad W., Shabbiri K., Adnan A. Exploration of respiratory chain of Nocardia asteroides: purification of succinate quinone oxidoreductase. J Membr Biol 2012, 245:89-95.
    • (2012) J Membr Biol , vol.245 , pp. 89-95
    • Ahmad, W.1    Shabbiri, K.2    Adnan, A.3
  • 16
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal Biochem 1987, 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 17
    • 2642523613 scopus 로고    scopus 로고
    • The power and the limitations of cross-species protein identification by mass spectrometry-driven sequence similarity searches
    • Habermann B., Oegema J., Sunyaev S., Shevchenko A. The power and the limitations of cross-species protein identification by mass spectrometry-driven sequence similarity searches. Mol Cell Proteomics 2004, 3:238-249.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 238-249
    • Habermann, B.1    Oegema, J.2    Sunyaev, S.3    Shevchenko, A.4
  • 18
    • 0038216710 scopus 로고    scopus 로고
    • Cellular and extracellular proteome analysis of Streptococcus mutans grown in a chemostat
    • Len A.C., Cordwell S.J., Harty D.W., Jacques N.A. Cellular and extracellular proteome analysis of Streptococcus mutans grown in a chemostat. Proteomics 2003, 3:627-646.
    • (2003) Proteomics , vol.3 , pp. 627-646
    • Len, A.C.1    Cordwell, S.J.2    Harty, D.W.3    Jacques, N.A.4
  • 19
    • 77956483547 scopus 로고    scopus 로고
    • Cytoplasmic- and extracellular-proteome analysis of Diplodia seriata: a phytopathogenic fungus involved in grapevine decline
    • Cobos R., Barreiro C., Mateos R.M., Coque J.J. Cytoplasmic- and extracellular-proteome analysis of Diplodia seriata: a phytopathogenic fungus involved in grapevine decline. Proteome Sci 2010, 8:46.
    • (2010) Proteome Sci , vol.8 , pp. 46
    • Cobos, R.1    Barreiro, C.2    Mateos, R.M.3    Coque, J.J.4
  • 22
    • 33745207094 scopus 로고    scopus 로고
    • Software for computational peptide identification from MS-MS data
    • Xu C., Ma B. Software for computational peptide identification from MS-MS data. Drug Discov Today 2006, 11:595-600.
    • (2006) Drug Discov Today , vol.11 , pp. 595-600
    • Xu, C.1    Ma, B.2
  • 23
    • 34548506519 scopus 로고    scopus 로고
    • De novo protein sequence analysis of Macaca mulatta
    • Tannu N.S., Hemby S.E. De novo protein sequence analysis of Macaca mulatta. BMC Genomics 2007, 8:270.
    • (2007) BMC Genomics , vol.8 , pp. 270
    • Tannu, N.S.1    Hemby, S.E.2
  • 26
    • 0034872325 scopus 로고    scopus 로고
    • Comparative immune response to PE and PE_PGRS antigens of Mycobacterium tuberculosis
    • Delogu G., Brennan M.J. Comparative immune response to PE and PE_PGRS antigens of Mycobacterium tuberculosis. Infect Immun 2001, 69:5606-5611.
    • (2001) Infect Immun , vol.69 , pp. 5606-5611
    • Delogu, G.1    Brennan, M.J.2
  • 27
    • 33947135278 scopus 로고    scopus 로고
    • Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX
    • Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., et al. Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX. J Bacteriol 2007, 189:2477-2486.
    • (2007) J Bacteriol , vol.189 , pp. 2477-2486
    • Lykidis, A.1    Mavromatis, K.2    Ivanova, N.3    Anderson, I.4    Land, M.5    DiBartolo, G.6
  • 28
    • 81555215181 scopus 로고    scopus 로고
    • Homology-driven proteomics of dinoflagellates with unsequenced genomes using MALDI-TOF/TOF and automated de novo sequencing
    • Wang D.Z., Li C., Xie Z.X., Dong H.P., Lin L., Hong H.S. Homology-driven proteomics of dinoflagellates with unsequenced genomes using MALDI-TOF/TOF and automated de novo sequencing. Evid Based Complement Alternat Med 2011, 2011:471020.
    • (2011) Evid Based Complement Alternat Med , vol.2011 , pp. 471020
    • Wang, D.Z.1    Li, C.2    Xie, Z.X.3    Dong, H.P.4    Lin, L.5    Hong, H.S.6
  • 29
    • 0032993486 scopus 로고    scopus 로고
    • Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human
    • Wei N., Deng X.W. Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human. Trends Genet 1999, 15:98-103.
    • (1999) Trends Genet , vol.15 , pp. 98-103
    • Wei, N.1    Deng, X.W.2
  • 30
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications
    • Liska A.J., Shevchenko A. Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications. Proteomics 2003, 3:19-28.
    • (2003) Proteomics , vol.3 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.