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Volumn 11, Issue 19, 2011, Pages 3935-3941

A reference map of the membrane proteome of Enterococcus faecalis

Author keywords

Blue native PAGE; Enterococcus faecalis; Membrane proteome; Microbiology; Nano LC ESI MS MS; Protein complex

Indexed keywords

MEMBRANE PROTEIN;

EID: 80053039270     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100103     Document Type: Article
Times cited : (17)

References (25)
  • 1
    • 67650744795 scopus 로고    scopus 로고
    • The ecology, epidemiology and virulence of Enterococcus
    • Fisher, K., Phillips, C., The ecology, epidemiology and virulence of Enterococcus. Microbiology 2009, 155, 1749-1757.
    • (2009) Microbiology , vol.155 , pp. 1749-1757
    • Fisher, K.1    Phillips, C.2
  • 3
    • 54949148412 scopus 로고    scopus 로고
    • NHSN annual update: antimicrobial-resistant pathogens associated with healthcare-associated infections: annual summary of data reported to the National Healthcare Safety Network at the Centers for Disease Control and Prevention 2006-2007
    • Hidron, A. I., Edwards, J. R., Patel, J., Horan, T. C. et al., NHSN annual update: antimicrobial-resistant pathogens associated with healthcare-associated infections: annual summary of data reported to the National Healthcare Safety Network at the Centers for Disease Control and Prevention 2006-2007. Infect. Control Hosp. Epidemiol. 2008, 29, 996-1011.
    • (2008) Infect. Control Hosp. Epidemiol. , vol.29 , pp. 996-1011
    • Hidron, A.I.1    Edwards, J.R.2    Patel, J.3    Horan, T.C.4
  • 4
    • 0037470983 scopus 로고    scopus 로고
    • Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis
    • Paulsen, I. T., Banerjei, L., Myers, G. S., Nelson, K. E. et al., Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science 2003, 299, 2071-2074.
    • (2003) Science , vol.299 , pp. 2071-2074
    • Paulsen, I.T.1    Banerjei, L.2    Myers, G.S.3    Nelson, K.E.4
  • 5
    • 48249085658 scopus 로고    scopus 로고
    • Large scale variation in Enterococcus faecalis illustrated by the genome analysis of strain OG1RF
    • Bourgogne, A., Garsin, D. A., Qin, X., Singh, K. V. et al., Large scale variation in Enterococcus faecalis illustrated by the genome analysis of strain OG1RF. Genome Biol. 2008, 9, R110.
    • (2008) Genome Biol. , vol.9
    • Bourgogne, A.1    Garsin, D.A.2    Qin, X.3    Singh, K.V.4
  • 6
    • 33750319466 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and how they get there
    • Scott, J. R., Barnett, T. C., Surface proteins of gram-positive bacteria and how they get there. Annu. Rev. Microbiol. 2006, 60, 397-423.
    • (2006) Annu. Rev. Microbiol. , vol.60 , pp. 397-423
    • Scott, J.R.1    Barnett, T.C.2
  • 7
    • 78650293305 scopus 로고    scopus 로고
    • Targeting bacterial membrane function: an underexploited mechanism for treating persistent infections
    • Hurdle, J. G., O'Neill, A. J., Chopra, I., Lee, R. E., Targeting bacterial membrane function: an underexploited mechanism for treating persistent infections. Nat. Rev. Microbiol. 2011, 9, 62-75.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 62-75
    • Hurdle, J.G.1    O'Neill, A.J.2    Chopra, I.3    Lee, R.E.4
  • 8
    • 69249131223 scopus 로고    scopus 로고
    • Identification of secreted and surface proteins from Enterococcus faecalis
    • Benachour, A., Morin, T., Hebert, L., Budin-Verneuil, A. et al., Identification of secreted and surface proteins from Enterococcus faecalis. Can. J. Microbiol. 2009, 55, 967-974.
    • (2009) Can. J. Microbiol. , vol.55 , pp. 967-974
    • Benachour, A.1    Morin, T.2    Hebert, L.3    Budin-Verneuil, A.4
  • 10
    • 0020823094 scopus 로고
    • Modification of Streptococcus faecalis sex pheromones after acquisition of plasmid DNA
    • Ike, Y., Craig, R. A., White, B. A., Yagi, Y., Clewell, D. B., Modification of Streptococcus faecalis sex pheromones after acquisition of plasmid DNA. Proc. Natl. Acad. Sci. USA 1983, 80, 5369-5373.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5369-5373
    • Ike, Y.1    Craig, R.A.2    White, B.A.3    Yagi, Y.4    Clewell, D.B.5
  • 11
    • 79953693293 scopus 로고    scopus 로고
    • Systematic analysis of native membrane protein complexes in Escherichia coli
    • Maddalo, G., Stenberg Bruzell, F., Gotzke, H., Toddo, S. et al., Systematic analysis of native membrane protein complexes in Escherichia coli. J. Proteome Res. 2011, 10, 1848-1859.
    • (2011) J. Proteome Res. , vol.10 , pp. 1848-1859
    • Maddalo, G.1    Stenberg Bruzell, F.2    Gotzke, H.3    Toddo, S.4
  • 13
    • 44449083478 scopus 로고    scopus 로고
    • Prediction of membrane-protein topology from first principles
    • Bernsel, A., Viklund, H., Falk, J., Lindahl, E. et al., Prediction of membrane-protein topology from first principles. Proc. Natl. Acad. Sci. USA 2008, 105, 7177-7181.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7177-7181
    • Bernsel, A.1    Viklund, H.2    Falk, J.3    Lindahl, E.4
  • 14
    • 61549096272 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in gram-positive bacteria with a Hidden Markov Model
    • Bagos, P. G., Tsirigos, K. D., Liakopoulos, T. D., Hamodrakas, S. J., Prediction of lipoprotein signal peptides in gram-positive bacteria with a Hidden Markov Model. J. Proteome Res. 2008, 7, 5082-5093.
    • (2008) J. Proteome Res. , vol.7 , pp. 5082-5093
    • Bagos, P.G.1    Tsirigos, K.D.2    Liakopoulos, T.D.3    Hamodrakas, S.J.4
  • 15
    • 77955134701 scopus 로고    scopus 로고
    • Identification of proteins related to the stress response in Enterococcus faecalis V583 caused by bovine bile
    • Bohle, L. A., Faergestad, E. M., Veiseth-Kent, E., Steinmoen, H. et al., Identification of proteins related to the stress response in Enterococcus faecalis V583 caused by bovine bile. Proteome Sci. 2010, 8, 37.
    • (2010) Proteome Sci. , vol.8 , pp. 37
    • Bohle, L.A.1    Faergestad, E.M.2    Veiseth-Kent, E.3    Steinmoen, H.4
  • 17
    • 0036889302 scopus 로고    scopus 로고
    • The viable but nonculturable state and starvation are different stress responses of Enterococcus faecalis, as determined by proteome analysis
    • Heim, S., Lleo, M. M., Bonato, B., Guzman, C. A., Canepari, P., The viable but nonculturable state and starvation are different stress responses of Enterococcus faecalis, as determined by proteome analysis. J. Bacteriol. 2002, 184, 6739-6745.
    • (2002) J. Bacteriol. , vol.184 , pp. 6739-6745
    • Heim, S.1    Lleo, M.M.2    Bonato, B.3    Guzman, C.A.4    Canepari, P.5
  • 18
    • 77950658284 scopus 로고    scopus 로고
    • Proteomic analysis of the Enterococcus faecalis V583 strain and clinical isolate V309 under vancomycin treatment
    • Wang, X., He, X., Jiang, Z., Wang, J. et al., Proteomic analysis of the Enterococcus faecalis V583 strain and clinical isolate V309 under vancomycin treatment. J. Proteome Res. 2010, 9, 1772-1785.
    • (2010) J. Proteome Res. , vol.9 , pp. 1772-1785
    • Wang, X.1    He, X.2    Jiang, Z.3    Wang, J.4
  • 19
    • 70349327690 scopus 로고    scopus 로고
    • Exploring the inner membrane proteome of Escherichia coli: which proteins are eluding detection and why?
    • Bernsel, A., Daley, D. O., Exploring the inner membrane proteome of Escherichia coli: which proteins are eluding detection and why? Trends Microbiol. 2009, 17, 444-449.
    • (2009) Trends Microbiol. , vol.17 , pp. 444-449
    • Bernsel, A.1    Daley, D.O.2
  • 20
    • 10944249586 scopus 로고    scopus 로고
    • Hiding behind hydrophobicity. Transmembrane segments in mass spectrometry
    • Eichacker, L. A., Granvogl, B., Mirus, O., Muller, B. C. et al., Hiding behind hydrophobicity. Transmembrane segments in mass spectrometry. J. Biol. Chem. 2004, 279, 50915-50922.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50915-50922
    • Eichacker, L.A.1    Granvogl, B.2    Mirus, O.3    Muller, B.C.4
  • 21
    • 33646557331 scopus 로고    scopus 로고
    • Protein cleavage strategies for an improved analysis of the membrane proteome
    • Fischer, F., Poetsch, A., Protein cleavage strategies for an improved analysis of the membrane proteome. Proteome Sci. 2006, 4, 2.
    • (2006) Proteome Sci. , vol.4 , pp. 2
    • Fischer, F.1    Poetsch, A.2
  • 22
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: un amour impossible?
    • Santoni, V., Molloy, M., Rabilloud, T., Membrane proteins and proteomics: un amour impossible? Electrophoresis 2000, 21, 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 23
    • 70349350617 scopus 로고    scopus 로고
    • Exploring membrane proteomes
    • in: Hagen, V. (Ed.), Wiley-VCH, Weinheim.
    • Stenberg, F., Daley, D. O., Exploring membrane proteomes. in: Hagen, V. (Ed.), Proteomics Sample Preparation, Wiley-VCH, Weinheim 2008, pp. 303-312.
    • (2008) Proteomics Sample Preparation , pp. 303-312
    • Stenberg, F.1    Daley, D.O.2
  • 24
    • 50049135906 scopus 로고    scopus 로고
    • Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis
    • Weiner, J. H., Li, L., Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis. Biochim. Biophys. Acta 2008, 1778, 1698-1713.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1698-1713
    • Weiner, J.H.1    Li, L.2
  • 25
    • 79953192195 scopus 로고    scopus 로고
    • Overcoming key technological challenges in using mass spectrometry for mapping cell surfaces in tissues
    • Griffin, N. M., Schnitzer, J. E., Overcoming key technological challenges in using mass spectrometry for mapping cell surfaces in tissues. Mol. Cell Proteomics 2011, 10, R110 000935.
    • (2011) Mol. Cell Proteomics , vol.10
    • Griffin, N.M.1    Schnitzer, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.