메뉴 건너뛰기




Volumn 11, Issue 15, 2011, Pages 3203-3211

Proteome analysis of host-pathogen interactions: Investigation of pathogen responses to the host cell environment

Author keywords

Bacterial adaptation responses; Enrichment strategies; In vivo proteomics; Infection biology; Microbiology

Indexed keywords

PROTEOME;

EID: 79960387002     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100158     Document Type: Review
Times cited : (62)

References (64)
  • 1
    • 12944302098 scopus 로고    scopus 로고
    • Lack of development of new antimicrobial drugs: a potential serious threat to public health
    • Norrby, S. R., Nord, C. E., Finch, R., Lack of development of new antimicrobial drugs: a potential serious threat to public health. Lancet Infect. Dis. 2005, 5, 115-119.
    • (2005) Lancet Infect. Dis. , vol.5 , pp. 115-119
    • Norrby, S.R.1    Nord, C.E.2    Finch, R.3
  • 2
    • 77957234670 scopus 로고    scopus 로고
    • Pathogen proteomes during infection: a basis for infection research and novel control strategies
    • Bumann, D., Pathogen proteomes during infection: a basis for infection research and novel control strategies. J. Proteomics 2010, 73, 2267-2276.
    • (2010) J. Proteomics , vol.73 , pp. 2267-2276
    • Bumann, D.1
  • 3
    • 44649147111 scopus 로고    scopus 로고
    • Proteomics of bacterial pathogens
    • Cash, P., Proteomics of bacterial pathogens. Expert Opin. Drug Discov. 2008, 3, 461-473.
    • (2008) Expert Opin. Drug Discov. , vol.3 , pp. 461-473
    • Cash, P.1
  • 4
    • 73649114530 scopus 로고    scopus 로고
    • A proteomic view of cell physiology and virulence of Staphylococcus aureus
    • Hecker, M., Becher, D., Fuchs, S., Engelmann, S., A proteomic view of cell physiology and virulence of Staphylococcus aureus. Int. J. Med. Microbiol. 2010, 300, 76-87.
    • (2010) Int. J. Med. Microbiol. , vol.300 , pp. 76-87
    • Hecker, M.1    Becher, D.2    Fuchs, S.3    Engelmann, S.4
  • 5
    • 35348918150 scopus 로고    scopus 로고
    • Understanding the physiology and adaptation of staphylococci: a post-genomic approach
    • Becker, K., Bierbaum, G., von Eiff, C., Engelmann, S. et al., Understanding the physiology and adaptation of staphylococci: a post-genomic approach. Int. J. Med. Microbiol. 2007, 297, 483-501.
    • (2007) Int. J. Med. Microbiol. , vol.297 , pp. 483-501
    • Becker, K.1    Bierbaum, G.2    von Eiff, C.3    Engelmann, S.4
  • 6
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • Betts, J. C., Lukey, P. T., Robb, L. C., McAdam, R. A., Duncan, K., Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol. Microbiol. 2002, 43, 717-731.
    • (2002) Mol. Microbiol. , vol.43 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    McAdam, R.A.4    Duncan, K.5
  • 7
    • 33846908531 scopus 로고    scopus 로고
    • Proteomic profiling of cellular stresses in Bacillus subtilis reveals cellular networks and assists in elucidating antibiotic mechanisms of action
    • Bandow, J. E., Hecker, M., Proteomic profiling of cellular stresses in Bacillus subtilis reveals cellular networks and assists in elucidating antibiotic mechanisms of action. Prog. Drug Res. 2007, 64, 81-101.
    • (2007) Prog. Drug Res. , vol.64 , pp. 81-101
    • Bandow, J.E.1    Hecker, M.2
  • 8
    • 27144460621 scopus 로고    scopus 로고
    • Dysregulation of bacterial proteolytic machinery by a new class of antibiotics
    • Brotz-Oesterhelt, H., Beyer, D., Kroll, H. P., Endermann, R. et al., Dysregulation of bacterial proteolytic machinery by a new class of antibiotics. Nat. Med. 2005, 11, 1082-1087.
    • (2005) Nat. Med. , vol.11 , pp. 1082-1087
    • Brotz-Oesterhelt, H.1    Beyer, D.2    Kroll, H.P.3    Endermann, R.4
  • 10
    • 59849095575 scopus 로고    scopus 로고
    • Use of high-throughput mass spectrometry to elucidate host-pathogen interactions in Salmonella
    • Rodland, K. D., Adkins, J. N., Ansong, C., Chowdhury, S. et al., Use of high-throughput mass spectrometry to elucidate host-pathogen interactions in Salmonella. Future Microbiol. 2008, 3, 625-634.
    • (2008) Future Microbiol. , vol.3 , pp. 625-634
    • Rodland, K.D.1    Adkins, J.N.2    Ansong, C.3    Chowdhury, S.4
  • 11
    • 33646266241 scopus 로고    scopus 로고
    • Proteins unique to intraphagosomally grown Mycobacterium tuberculosis
    • Mattow, J., Siejak, F., Hagens, K., Becher, D. et al., Proteins unique to intraphagosomally grown Mycobacterium tuberculosis. Proteomics 2006, 6, 2485-2494.
    • (2006) Proteomics , vol.6 , pp. 2485-2494
    • Mattow, J.1    Siejak, F.2    Hagens, K.3    Becher, D.4
  • 12
    • 0017861127 scopus 로고
    • Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates
    • Pedersen, S., Bloch, P. L., Reeh, S., Neidhardt, F. C., Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates. Cell 1978, 14, 179-190.
    • (1978) Cell , vol.14 , pp. 179-190
    • Pedersen, S.1    Bloch, P.L.2    Reeh, S.3    Neidhardt, F.C.4
  • 13
    • 0027167444 scopus 로고
    • Analysis of proteins synthesized by Salmonella typhimurium during growth within a host macrophage
    • Abshire, K. Z., Neidhardt, F. C., Analysis of proteins synthesized by Salmonella typhimurium during growth within a host macrophage. J. Bacteriol. 1993, 175, 3734-3743.
    • (1993) J. Bacteriol. , vol.175 , pp. 3734-3743
    • Abshire, K.Z.1    Neidhardt, F.C.2
  • 14
    • 0021637305 scopus 로고
    • Two-dimensional electrophoresis used to differentiate the causal agents of American tegumentary leishmaniasis
    • Saravia, N. G., Gemmell, M. A., Nance, S. L., Anderson, N. L., Two-dimensional electrophoresis used to differentiate the causal agents of American tegumentary leishmaniasis. Clin. Chem. 1984, 30, 2048-2052.
    • (1984) Clin. Chem. , vol.30 , pp. 2048-2052
    • Saravia, N.G.1    Gemmell, M.A.2    Nance, S.L.3    Anderson, N.L.4
  • 15
    • 0025294798 scopus 로고
    • Induction of Salmonella stress proteins upon infection of macrophages
    • Buchmeier, N. A., Heffron, F., Induction of Salmonella stress proteins upon infection of macrophages. Science 1990, 248, 730-732.
    • (1990) Science , vol.248 , pp. 730-732
    • Buchmeier, N.A.1    Heffron, F.2
  • 16
    • 77949517375 scopus 로고    scopus 로고
    • A proteomic view of an important human pathogen - towards the quantification of the entire Staphylococcus aureus proteome
    • Becher, D., Hempel, K., Sievers, S., Zühlke, D. et al., A proteomic view of an important human pathogen - towards the quantification of the entire Staphylococcus aureus proteome. PLoS One 2009, 4, e8176.
    • (2009) PLoS One , vol.4
    • Becher, D.1    Hempel, K.2    Sievers, S.3    Zühlke, D.4
  • 17
    • 68449102172 scopus 로고    scopus 로고
    • Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
    • Malmstrom, J., Beck, M., Schmidt, A., Lange, V. et al., Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans. Nature 2009, 460, 762-765.
    • (2009) Nature , vol.460 , pp. 762-765
    • Malmstrom, J.1    Beck, M.2    Schmidt, A.3    Lange, V.4
  • 18
    • 0037143692 scopus 로고    scopus 로고
    • Global analysis of the Deinococcus radiodurans proteome by using accurate mass tags
    • Lipton, M. S., Pasa-Tolic, L., Anderson, G. A., Anderson, D. J. et al., Global analysis of the Deinococcus radiodurans proteome by using accurate mass tags. Proc. Natl. Acad. Sci. USA 2002, 99, 11049-11054.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11049-11054
    • Lipton, M.S.1    Pasa-Tolic, L.2    Anderson, G.A.3    Anderson, D.J.4
  • 19
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: the protein inference problem
    • Nesvizhskii, A. I., Aebersold, R., Interpretation of shotgun proteomic data: the protein inference problem. Mol. Cell. Proteomics 2005, 4, 1419-1440.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 20
    • 0027417230 scopus 로고
    • Phenotypic modulation by Legionella pneumophila upon infection of macrophages
    • Abu Kwaik, Y., Eisenstein, B. I., Engleberg, N. C., Phenotypic modulation by Legionella pneumophila upon infection of macrophages. Infect. Immun. 1993, 61, 1320-1329.
    • (1993) Infect. Immun. , vol.61 , pp. 1320-1329
    • Abu Kwaik, Y.1    Eisenstein, B.I.2    Engleberg, N.C.3
  • 21
    • 0028826678 scopus 로고
    • Listeria monocytogenes can grow in macrophages without the aid of proteins induced by environmental stresses
    • Hanawa, T., Yamamoto, T., Kamiya, S., Listeria monocytogenes can grow in macrophages without the aid of proteins induced by environmental stresses. Infect. Immun. 1995, 63, 4595-4599.
    • (1995) Infect. Immun. , vol.63 , pp. 4595-4599
    • Hanawa, T.1    Yamamoto, T.2    Kamiya, S.3
  • 22
    • 34147124324 scopus 로고    scopus 로고
    • Integrated proteomics and genomics strategies bring new insight into Candida albicans response upon macrophage interaction
    • Fernandez-Arenas, E., Cabezon, V., Bermejo, C., Arroyo, J. et al., Integrated proteomics and genomics strategies bring new insight into Candida albicans response upon macrophage interaction. Mol. Cell. Proteomics 2007, 6, 460-478.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 460-478
    • Fernandez-Arenas, E.1    Cabezon, V.2    Bermejo, C.3    Arroyo, J.4
  • 23
    • 32944469752 scopus 로고    scopus 로고
    • Analysis of the Pasteurella multocida outer membrane sub-proteome and its response to the in vivo environment of the natural host
    • Boyce, J. D., Cullen, P. A., Nguyen, V., Wilkie, I., Adler, B., Analysis of the Pasteurella multocida outer membrane sub-proteome and its response to the in vivo environment of the natural host. Proteomics 2006, 6, 870-880.
    • (2006) Proteomics , vol.6 , pp. 870-880
    • Boyce, J.D.1    Cullen, P.A.2    Nguyen, V.3    Wilkie, I.4    Adler, B.5
  • 24
    • 0030990845 scopus 로고    scopus 로고
    • 3rd, Specific detection of Salmonella typhimurium proteins synthesized intracellularly
    • Burns-Keliher, L. L., Portteus, A., Curtiss, R., 3rd, Specific detection of Salmonella typhimurium proteins synthesized intracellularly. J. Bacteriol. 1997, 179, 3604-3612.
    • (1997) J. Bacteriol. , vol.179 , pp. 3604-3612
    • Burns-Keliher, L.L.1    Portteus, A.2    Curtiss, R.3
  • 25
    • 0028826678 scopus 로고
    • Listeria monocytogenes can grow in macrophages without the aid of proteins induced by environmental stresses
    • Hanawa, T., Yamamoto, T., Kamiya, S., Listeria monocytogenes can grow in macrophages without the aid of proteins induced by environmental stresses. Infect. Immun. 1995, 63, 4595-4599.
    • (1995) Infect. Immun. , vol.63 , pp. 4595-4599
    • Hanawa, T.1    Yamamoto, T.2    Kamiya, S.3
  • 26
    • 0026492055 scopus 로고
    • Altered synthetic response of Campylobacter jejuni to cocultivation with human epithelial cells is associated with enhanced internalization
    • Konkel, M. E., Cieplak, W., Jr, Altered synthetic response of Campylobacter jejuni to cocultivation with human epithelial cells is associated with enhanced internalization. Infect. Immun. 1992, 60, 4945-4949.
    • (1992) Infect. Immun. , vol.60 , pp. 4945-4949
    • Konkel, M.E.1    Cieplak Jr, W.2
  • 27
    • 0028265798 scopus 로고
    • Induction of Yersinia enterocolitica stress proteins by phagocytosis with macrophage
    • Yamamoto, T., Hanawa, T., Ogata, S., Induction of Yersinia enterocolitica stress proteins by phagocytosis with macrophage. Microbiol. Immunol. 1994, 38, 295-300.
    • (1994) Microbiol. Immunol. , vol.38 , pp. 295-300
    • Yamamoto, T.1    Hanawa, T.2    Ogata, S.3
  • 28
    • 37049009528 scopus 로고    scopus 로고
    • Quantitative proteomics of intracellular Porphyromonas gingivalis
    • Xia, Q., Wang, T., Taub, F., Park, Y. et al., Quantitative proteomics of intracellular Porphyromonas gingivalis. Proteomics 2007, 7, 4323-4337.
    • (2007) Proteomics , vol.7 , pp. 4323-4337
    • Xia, Q.1    Wang, T.2    Taub, F.3    Park, Y.4
  • 29
    • 79954442166 scopus 로고    scopus 로고
    • In vivo studies of Clostridium perfringens in mouse gas gangrene model
    • Sengupta, N., Alam, S. I., In vivo studies of Clostridium perfringens in mouse gas gangrene model. Curr. Microbiol. 2011, 62, 999-1008.
    • (2011) Curr. Microbiol. , vol.62 , pp. 999-1008
    • Sengupta, N.1    Alam, S.I.2
  • 30
    • 33749424678 scopus 로고    scopus 로고
    • Proteomic analysis of Salmonella enterica serovar typhimurium isolated from RAW 264.7 macrophages: identification of a novel protein that contributes to the replication of serovar typhimurium inside macrophages
    • Shi, L., Adkins, J. N., Coleman, J. R., Schepmoes, A. A. et al., Proteomic analysis of Salmonella enterica serovar typhimurium isolated from RAW 264.7 macrophages: identification of a novel protein that contributes to the replication of serovar typhimurium inside macrophages. J. Biol. Chem. 2006, 281, 29131-29140.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29131-29140
    • Shi, L.1    Adkins, J.N.2    Coleman, J.R.3    Schepmoes, A.A.4
  • 31
    • 33744548258 scopus 로고    scopus 로고
    • In vivo proteomic analysis of the intracellular bacterial pathogen, Francisella tularensis, isolated from mouse spleen
    • Twine, S. M., Mykytczuk, N. C., Petit, M. D., Shen, H. et al., In vivo proteomic analysis of the intracellular bacterial pathogen, Francisella tularensis, isolated from mouse spleen. Biochem. Biophys. Res. Commun. 2006, 345, 1621-1633.
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 1621-1633
    • Twine, S.M.1    Mykytczuk, N.C.2    Petit, M.D.3    Shen, H.4
  • 32
    • 33645030241 scopus 로고    scopus 로고
    • Robust Salmonella metabolism limits possibilities for new antimicrobials
    • Becker, D., Selbach, M., Rollenhagen, C., Ballmaier, M. et al., Robust Salmonella metabolism limits possibilities for new antimicrobials. Nature 2006, 440, 303-307.
    • (2006) Nature , vol.440 , pp. 303-307
    • Becker, D.1    Selbach, M.2    Rollenhagen, C.3    Ballmaier, M.4
  • 33
    • 52649088373 scopus 로고    scopus 로고
    • Transgenic, fluorescent Leishmania mexicana allow direct analysis of the proteome of intracellular amastigotes
    • Paape, D., Lippuner, C., Schmid, M., Ackermann, R. et al., Transgenic, fluorescent Leishmania mexicana allow direct analysis of the proteome of intracellular amastigotes. Mol. Cell. Proteomics 2008, 7, 1688-1701.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1688-1701
    • Paape, D.1    Lippuner, C.2    Schmid, M.3    Ackermann, R.4
  • 35
    • 77955119702 scopus 로고    scopus 로고
    • Time-resolved quantitative proteome profiling of host-pathogen interactions: The response of Staphylococcus aureus RN1HG to internalisation by human airway epithelial cells
    • Schmidt, F., Scharf, S. S., Hildebrandt, P., Burian, M. et al., Time-resolved quantitative proteome profiling of host-pathogen interactions: The response of Staphylococcus aureus RN1HG to internalisation by human airway epithelial cells. Proteomics 2010, 10, 2801-2811.
    • (2010) Proteomics , vol.10 , pp. 2801-2811
    • Schmidt, F.1    Scharf, S.S.2    Hildebrandt, P.3    Burian, M.4
  • 36
    • 33845230421 scopus 로고    scopus 로고
    • A cytomic approach reveals population heterogeneity of Cupriavidus necator in response to harmful phenol concentrations
    • Wiacek, C., Muller, S., Benndorf, D., A cytomic approach reveals population heterogeneity of Cupriavidus necator in response to harmful phenol concentrations. Proteomics 2006, 6, 5983-5994.
    • (2006) Proteomics , vol.6 , pp. 5983-5994
    • Wiacek, C.1    Muller, S.2    Benndorf, D.3
  • 37
    • 33846318560 scopus 로고    scopus 로고
    • Proteomic comparison of Mycobacterium avium subspecies paratuberculosis grown in vitro and isolated from clinical cases of ovine paratuberculosis
    • Hughes, V., Smith, S., Garcia-Sanchez, A., Sales, J., Stevenson, K., Proteomic comparison of Mycobacterium avium subspecies paratuberculosis grown in vitro and isolated from clinical cases of ovine paratuberculosis. Microbiology 2007, 153, 196-205.
    • (2007) Microbiology , vol.153 , pp. 196-205
    • Hughes, V.1    Smith, S.2    Garcia-Sanchez, A.3    Sales, J.4    Stevenson, K.5
  • 38
    • 53549123036 scopus 로고    scopus 로고
    • Quantitative analysis of the intramacrophagic Brucella suis proteome reveals metabolic adaptation to late stage of cellular infection
    • Al Dahouk, S., Jubier-Maurin, V., Scholz, H. C., Tomaso, H. et al., Quantitative analysis of the intramacrophagic Brucella suis proteome reveals metabolic adaptation to late stage of cellular infection. Proteomics 2008, 8, 3862-3870.
    • (2008) Proteomics , vol.8 , pp. 3862-3870
    • Al Dahouk, S.1    Jubier-Maurin, V.2    Scholz, H.C.3    Tomaso, H.4
  • 39
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G., Yates, J. R., 3rd, A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 2004, 76, 4193-4201.
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates 3rd, J.R.3
  • 40
    • 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. et al., 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 2005, 4, 1265-1272.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4
  • 41
    • 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. et al., Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 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
  • 42
    • 77950670379 scopus 로고    scopus 로고
    • Analysis of detergent-insoluble and whole cell lysate fractions of resting neutrophils using high-resolution mass spectrometry
    • Tomazella, G. G., daSilva, I., Thome, C. H., Greene, L. J. et al., Analysis of detergent-insoluble and whole cell lysate fractions of resting neutrophils using high-resolution mass spectrometry. J. Proteome Res. 2010, 9, 2030-2036.
    • (2010) J. Proteome Res. , vol.9 , pp. 2030-2036
    • Tomazella, G.G.1    daSilva, I.2    Thome, C.H.3    Greene, L.J.4
  • 43
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., Gygi, S. P., Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. USA 2003, 100, 6940-6945.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 44
    • 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. et al., Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 2002, 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
  • 46
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF
    • Wu, W. W., Wang, G., Baek, S. J., Shen, R. F., Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF. J. Proteome Res. 2006, 5, 651-658.
    • (2006) J. Proteome Res. , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.2    Baek, S.J.3    Shen, R.F.4
  • 47
    • 41149127192 scopus 로고    scopus 로고
    • A label-free quantification method by MS/MS TIC compared to SILAC and spectral counting in a proteomics screen
    • Asara, J. M., Christofk, H. R., Freimark, L. M., Cantley, L. C., A label-free quantification method by MS/MS TIC compared to SILAC and spectral counting in a proteomics screen. Proteomics 2008, 8, 994-999.
    • (2008) Proteomics , vol.8 , pp. 994-999
    • Asara, J.M.1    Christofk, H.R.2    Freimark, L.M.3    Cantley, L.C.4
  • 48
    • 2542574741 scopus 로고    scopus 로고
    • Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology
    • Schmidt, F., Donahoe, S., Hagens, K., Mattow, J. et al., Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology. Mol. Cell. Proteomics 2004, 3, 24-42.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 24-42
    • Schmidt, F.1    Donahoe, S.2    Hagens, K.3    Mattow, J.4
  • 49
    • 27644543078 scopus 로고    scopus 로고
    • Comparison of label-free methods for quantifying human proteins by shotgun proteomics
    • Old, W. M., Meyer-Arendt, K., Aveline-Wolf, L., Pierce, K. G. et al., Comparison of label-free methods for quantifying human proteins by shotgun proteomics. Mol. Cell. Proteomics 2005, 4, 1487-1502.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1487-1502
    • Old, W.M.1    Meyer-Arendt, K.2    Aveline-Wolf, L.3    Pierce, K.G.4
  • 50
    • 78649738763 scopus 로고    scopus 로고
    • Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo
    • Kruh, N. A., Troudt, J., Izzo, A., Prenni, J., Dobos, K. M., Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. PLoS One 2010, 5, e13938.
    • (2010) PLoS One , vol.5
    • Kruh, N.A.1    Troudt, J.2    Izzo, A.3    Prenni, J.4    Dobos, K.M.5
  • 51
    • 70549084975 scopus 로고    scopus 로고
    • Directed mass spectrometry: towards hypothesis-driven proteomics
    • Schmidt, A., Claassen, M., Aebersold, R., Directed mass spectrometry: towards hypothesis-driven proteomics. Curr. Opin. Chem. Biol. 2009, 13, 510-517.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 510-517
    • Schmidt, A.1    Claassen, M.2    Aebersold, R.3
  • 52
    • 79953227740 scopus 로고    scopus 로고
    • Increased selectivity, analytical precision, and throughput in targeted proteomics
    • Kiyonami, R., Schoen, A., Prakash, A., Peterman, S. et al., Increased selectivity, analytical precision, and throughput in targeted proteomics. Mol. Cell. Proteomics 2011, 10, M110.002931.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Kiyonami, R.1    Schoen, A.2    Prakash, A.3    Peterman, S.4
  • 53
    • 74049131716 scopus 로고    scopus 로고
    • High-throughput generation of selected reaction-monitoring assays for proteins and proteomes
    • Picotti, P., Rinner, O., Stallmach, R., Dautel, F. et al., High-throughput generation of selected reaction-monitoring assays for proteins and proteomes. Nat. Methods 2010, 7, 43-46.
    • (2010) Nat. Methods , vol.7 , pp. 43-46
    • Picotti, P.1    Rinner, O.2    Stallmach, R.3    Dautel, F.4
  • 54
    • 43049090085 scopus 로고    scopus 로고
    • Targeted quantitative analysis of Streptococcus pyogenes virulence factors by multiple reaction monitoring
    • Lange, V., Malmstrom, J. A., Didion, J., King, N. L. et al., Targeted quantitative analysis of Streptococcus pyogenes virulence factors by multiple reaction monitoring. Mol. Cell. Proteomics 2008, 7, 1489-1500.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1489-1500
    • Lange, V.1    Malmstrom, J.A.2    Didion, J.3    King, N.L.4
  • 55
    • 78449274207 scopus 로고    scopus 로고
    • Analysis of phagosomal proteomes: from latex-bead to bacterial phagosomes
    • Li, Q., Jagannath, C., Rao, P. K., Singh, C. R., Lostumbo, G., Analysis of phagosomal proteomes: from latex-bead to bacterial phagosomes. Proteomics 2010, 10, 4098-4116.
    • (2010) Proteomics , vol.10 , pp. 4098-4116
    • Li, Q.1    Jagannath, C.2    Rao, P.K.3    Singh, C.R.4    Lostumbo, G.5
  • 56
    • 77951138081 scopus 로고    scopus 로고
    • Never take candy from a stranger: the role of the bacterial glycome in host-pathogen interactions
    • Reid, C. W., Fulton, K. M., Twine, S. M., Never take candy from a stranger: the role of the bacterial glycome in host-pathogen interactions. Future Microbiol. 2010, 5, 267-288.
    • (2010) Future Microbiol. , vol.5 , pp. 267-288
    • Reid, C.W.1    Fulton, K.M.2    Twine, S.M.3
  • 57
    • 0029820565 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens
    • Wizemann, T. M., Moskovitz, J., Pearce, B. J., Cundell, D. et al., Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens. Proc. Natl. Acad. Sci. USA 1996, 93, 7985-7990.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7985-7990
    • Wizemann, T.M.1    Moskovitz, J.2    Pearce, B.J.3    Cundell, D.4
  • 58
    • 26944462004 scopus 로고    scopus 로고
    • Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis
    • Hochgrafe, F., Mostertz, J., Albrecht, D., Hecker, M., Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis. Mol. Microbiol. 2005, 58, 409-425.
    • (2005) Mol. Microbiol. , vol.58 , pp. 409-425
    • Hochgrafe, F.1    Mostertz, J.2    Albrecht, D.3    Hecker, M.4
  • 59
    • 46149125288 scopus 로고    scopus 로고
    • Quantifying changes in the thiol redox proteome upon oxidative stress in vivo
    • Leichert, L. I., Gehrke, F., Gudiseva, H. V., Blackwell, T. et al., Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc. Natl. Acad. Sci. USA 2008, 105, 8197-8202.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8197-8202
    • Leichert, L.I.1    Gehrke, F.2    Gudiseva, H.V.3    Blackwell, T.4
  • 60
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang, Q., Zhang, Y., Yang, C., Xiong, H. et al., Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 2010, 327, 1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4
  • 61
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: principles and applications
    • Macek, B., Mann, M., Olsen, J. V., Global and site-specific quantitative phosphoproteomics: principles and applications. Annu. Rev. Pharmacol. Toxicol. 2009, 49, 199-221.
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 62
    • 33748322018 scopus 로고    scopus 로고
    • Analysis of the Salmonella typhimurium proteome through environmental response toward infectious conditions
    • Adkins, J. N., Mottaz, H. M., Norbeck, A. D., Gustin, J. K. et al., Analysis of the Salmonella typhimurium proteome through environmental response toward infectious conditions. Mol. Cell. Proteomics 2006, 5, 1450-1461.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1450-1461
    • Adkins, J.N.1    Mottaz, H.M.2    Norbeck, A.D.3    Gustin, J.K.4
  • 63
    • 70349686671 scopus 로고    scopus 로고
    • Systems integration of biodefense omics data for analysis of pathogen-host interactions and identification of potential targets
    • McGarvey, P. B., Huang, H., Mazumder, R., Zhang, J. et al., Systems integration of biodefense omics data for analysis of pathogen-host interactions and identification of potential targets. PLoS One 2009, 4, e7162.
    • (2009) PLoS One , vol.4
    • McGarvey, P.B.1    Huang, H.2    Mazumder, R.3    Zhang, J.4
  • 64
    • 77957192821 scopus 로고    scopus 로고
    • Using a label-free proteomics method to identify differentially abundant proteins in closely related hypo- and hypervirulent clinical Mycobacterium tuberculosis Beijing isolates
    • de Souza, G. A., Fortuin, S., Aguilar, D., Pando, R. H. et al., Using a label-free proteomics method to identify differentially abundant proteins in closely related hypo- and hypervirulent clinical Mycobacterium tuberculosis Beijing isolates. Mol. Cell. Proteomics 2010, 9, 2414-2423.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2414-2423
    • de Souza, G.A.1    Fortuin, S.2    Aguilar, D.3    Pando, R.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.