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Volumn 8, Issue 4, 2008, Pages 852-873

Application of proteomics technology for analyzing the interactions between host cells and intracellular infectious agents

Author keywords

Biomolecular interaction analysis; Host pathogen interaction; Interaction profiling; Protein differential expression; Proteomics methods

Indexed keywords

APOPTOSIS; CELL FRACTIONATION; CELL FUNCTION; CYTOSKELETON; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HOST CELL; HOST PATHOGEN INTERACTION; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IMMUNE RESPONSE; IMMUNOPRECIPITATION; IMMUNOSURVEILLANCE; MAJOR HISTOCOMPATIBILITY COMPLEX; MASS SPECTROMETRY; NONHUMAN; PATHOGENESIS; PATHOGENICITY; PHAGOCYTOSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEOMICS; REVIEW; SEVERE ACUTE RESPIRATORY SYNDROME; TWO DIMENSIONAL GEL ELECTROPHORESIS; VIRULENCE;

EID: 40549135956     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700664     Document Type: Review
Times cited : (33)

References (205)
  • 2
    • 0038299654 scopus 로고    scopus 로고
    • HIV-1 pathogenesis
    • Stevenson, M., HIV-1 pathogenesis. Nat. Med. 2003, 9, 853-860.
    • (2003) Nat. Med , vol.9 , pp. 853-860
    • Stevenson, M.1
  • 3
    • 0036062256 scopus 로고    scopus 로고
    • Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy
    • Greene, W. C., Peterlin, B. M., Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy. Nat. Med. 2002, 8, 673-680.
    • (2002) Nat. Med , vol.8 , pp. 673-680
    • Greene, W.C.1    Peterlin, B.M.2
  • 4
    • 0004124711 scopus 로고    scopus 로고
    • Nathanson, N, Ed, Lippincott-Raven, Philadelphia
    • Hardwick, J. M., Griffin, D. E., in: Nathanson, N. (Ed.), Viral pathogenesis, Lippincott-Raven, Philadelphia 1997, pp. 55-84.
    • (1997) Viral pathogenesis , pp. 55-84
    • Hardwick, J.M.1    Griffin, D.E.2
  • 5
    • 0023071706 scopus 로고
    • Impact of virus infection on host cell protein synthesis
    • Schneider, R. J., Shenk, T., Impact of virus infection on host cell protein synthesis. Annu. Rev. Biochem. 1987, 56, 317-332.
    • (1987) Annu. Rev. Biochem , vol.56 , pp. 317-332
    • Schneider, R.J.1    Shenk, T.2
  • 7
    • 0025872515 scopus 로고
    • HIV enhancer activity perpetuated by NF-kappa B induction on infection of monocytes
    • Bachelerie, F., Alcami, J., Arenzana-Seisdedos, F., Virelizier, J. L., HIV enhancer activity perpetuated by NF-kappa B induction on infection of monocytes. Nature 1991, 350, 709-712.
    • (1991) Nature , vol.350 , pp. 709-712
    • Bachelerie, F.1    Alcami, J.2    Arenzana-Seisdedos, F.3    Virelizier, J.L.4
  • 8
    • 33646166525 scopus 로고    scopus 로고
    • Intracellular restriction factors in mammalian cells - An ancient defense system finds a modern foe
    • Baumann, J. G., Intracellular restriction factors in mammalian cells - An ancient defense system finds a modern foe. Curr. HIV Res. 2006, 4, 141-168.
    • (2006) Curr. HIV Res , vol.4 , pp. 141-168
    • Baumann, J.G.1
  • 9
    • 34347225099 scopus 로고    scopus 로고
    • Virus and cell control
    • The dsRNA protein kinase PKR:, in press
    • Garcia, M. A., Meurs, E. F., Esteban, M., The dsRNA protein kinase PKR: Virus and cell control. Biochimie 2007, (in press).
    • (2007) Biochimie
    • Garcia, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 10
    • 27244444559 scopus 로고    scopus 로고
    • retroviral restriction and antiviral defence
    • TRIM family proteins
    • Nisole, S., Stoye, J. P., Saib, A., TRIM family proteins: retroviral restriction and antiviral defence. Nat. Rev. Microbiol. 2005, 3, 799-808.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 11
    • 33646825049 scopus 로고    scopus 로고
    • APOBEC3 cytidine deaminases: Distinct antiviral actions along the retroviral life cycle
    • Chiu, Y. L., Greene, W. C., APOBEC3 cytidine deaminases: distinct antiviral actions along the retroviral life cycle. J. Biol. Chem. 2006, 281, 8309-8312.
    • (2006) J. Biol. Chem , vol.281 , pp. 8309-8312
    • Chiu, Y.L.1    Greene, W.C.2
  • 12
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • Alcami, A., Viral mimicry of cytokines, chemokines and their receptors. Nat. Rev. Immunol. 2003, 3, 36-50.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 36-50
    • Alcami, A.1
  • 13
    • 27144449926 scopus 로고    scopus 로고
    • NK cell receptors involved in the response to human cytomegalovirus infection
    • Guma, M., Angulo, A., Lopez-Botet, M., NK cell receptors involved in the response to human cytomegalovirus infection. Curr. Top. Microbiol. Immunol. 2006, 298, 207-223.
    • (2006) Curr. Top. Microbiol. Immunol , vol.298 , pp. 207-223
    • Guma, M.1    Angulo, A.2    Lopez-Botet, M.3
  • 15
    • 0034283057 scopus 로고    scopus 로고
    • Viral mechanisms of immune evasion
    • Alcami, A., Koszinowski, U. H., Viral mechanisms of immune evasion. Trends Microbiol. 2000, 8, 410-418.
    • (2000) Trends Microbiol , vol.8 , pp. 410-418
    • Alcami, A.1    Koszinowski, U.H.2
  • 16
    • 5144233488 scopus 로고    scopus 로고
    • Strategies and mechanisms for host and pathogen survival in acute and persistent viral infections
    • Hilleman, M. R., Strategies and mechanisms for host and pathogen survival in acute and persistent viral infections. Proc. Natl. Acad. Sci. USA 2004, 101, Suppl 2, 14560-14566.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.SUPPL. 2 , pp. 14560-14566
    • Hilleman, M.R.1
  • 17
    • 0942265524 scopus 로고    scopus 로고
    • Proteomics in vaccinology and immunobiology: An informatics perspective of the immunone
    • Doytchinova, I. A., Taylor, P., Flower, D. R., Proteomics in vaccinology and immunobiology: An informatics perspective of the immunone. J. Biomed. Biotechnol. 2003, 5, 267-290.
    • (2003) J. Biomed. Biotechnol , vol.5 , pp. 267-290
    • Doytchinova, I.A.1    Taylor, P.2    Flower, D.R.3
  • 18
    • 1242284157 scopus 로고    scopus 로고
    • Proteomic and gene profiling approaches to study host responses to bacterial infection
    • Walduck, A., Rudel, T., Meyer, T. F., Proteomic and gene profiling approaches to study host responses to bacterial infection. Curr. Opin. Microbiol. 2004, 7, 33-38.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 33-38
    • Walduck, A.1    Rudel, T.2    Meyer, T.F.3
  • 19
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H., High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975, 250, 4007-4021.
    • (1975) J. Biol. Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 20
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., Whitehouse C. M., Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246, 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 21
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas, M., Hillenkamp, F., Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 1988, 60, 2299-2301.
    • (1988) Anal. Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 22
    • 0032924894 scopus 로고    scopus 로고
    • Advances in protein solubilisation for two-dimensional electrophoresis
    • Herbert, B., Advances in protein solubilisation for two-dimensional electrophoresis. Electrophoresis 1999, 20, 660-663.
    • (1999) Electrophoresis , vol.20 , pp. 660-663
    • Herbert, B.1
  • 23
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Görg, A., Weiss, W., Dunn, M. J., Current two-dimensional electrophoresis technology for proteomics. Proteomics 2004, 4, 3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Görg, A.1    Weiss, W.2    Dunn, M.J.3
  • 24
    • 17144475356 scopus 로고    scopus 로고
    • Zhang, C. G., Chromy, B. A., McCutchen-Maloney, S. L., Host-pathogen interactions: a proteomic view. Expert Rev. Proteomics 2005, 2, 187-202.
    • Zhang, C. G., Chromy, B. A., McCutchen-Maloney, S. L., Host-pathogen interactions: a proteomic view. Expert Rev. Proteomics 2005, 2, 187-202.
  • 25
    • 33847202974 scopus 로고    scopus 로고
    • Use of monolithic supports in proteomics technology
    • Josic, D., Clifton, J. G., Use of monolithic supports in proteomics technology. J. Chromatogr. A. 2007, 1144, 2-13.
    • (2007) J. Chromatogr. A , vol.1144 , pp. 2-13
    • Josic, D.1    Clifton, J.G.2
  • 26
    • 13844276803 scopus 로고    scopus 로고
    • Pre-fractionation techniques in proteome analysis: The mining tools of the third millennium
    • Righetti, P. G., Castagna, A., Antonioli, P., Boschetti, E., Pre-fractionation techniques in proteome analysis: the mining tools of the third millennium. Electrophoresis 2005, 26, 297-319.
    • (2005) Electrophoresis , vol.26 , pp. 297-319
    • Righetti, P.G.1    Castagna, A.2    Antonioli, P.3    Boschetti, E.4
  • 27
    • 0034630358 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients
    • Molloy, M. P., Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients. Anal. Biochem. 2000, 280, 1-10.
    • (2000) Anal. Biochem , vol.280 , pp. 1-10
    • Molloy, M.P.1
  • 28
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C. et al., Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases.Proc. Natl. Acad. Sci. USA 1993, 90, 5011-5015.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4
  • 30
    • 0001341506 scopus 로고
    • Collision-induced decompositions of aromatic molecular ions
    • Jennings, K. R., Collision-induced decompositions of aromatic molecular ions. Int. J. Mass Spectrom. Ion Phys. 1968, 1, 227-235.
    • (1968) Int. J. Mass Spectrom. Ion Phys , vol.1 , pp. 227-235
    • Jennings, K.R.1
  • 31
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., Mann, M., Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 32
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., Yates, J. R. III, Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19, 242-247.
    • (2001) Nat. Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 33
    • 7044237455 scopus 로고    scopus 로고
    • Proteome analysis of rhoptry-enriched fractions isolated from Plasmodium merozoites
    • Sam-Yellowe, T. Y., Florens, L., Wang, T., Raine, J. D. et al., Proteome analysis of rhoptry-enriched fractions isolated from Plasmodium merozoites. J. Proteome Res. 2004, 3, 995-1001.
    • (2004) J. Proteome Res , vol.3 , pp. 995-1001
    • Sam-Yellowe, T.Y.1    Florens, L.2    Wang, T.3    Raine, J.D.4
  • 34
    • 17844384255 scopus 로고    scopus 로고
    • Shotgun proteomic analysis of Chlamydia trachomatis
    • Skipp, P., Robinson, J., O'Connor, C. D., Clarke, I. N., Shotgun proteomic analysis of Chlamydia trachomatis. Proteomics 2005, 5, 1558-1573.
    • (2005) Proteomics , vol.5 , pp. 1558-1573
    • Skipp, P.1    Robinson, J.2    O'Connor, C.D.3    Clarke, I.N.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., Guilhaus, M., A proteomic view of Bifidobacterium infantis generated by multi-dimensional chromatography coupled with tandem mass spectrometry. Proteomics 2005, 5, 1859-1867.
    • (2005) Proteomics , vol.5 , pp. 1859-1867
    • Vitali, B.1    Wasinger, V.2    Brigidi, P.3    Guilhaus, M.4
  • 36
    • 34548024598 scopus 로고    scopus 로고
    • Integrating physical and genetic maps: From genomes to interaction networks
    • Beyer, A., Bandyopadhyay, S., Ideker, T., Integrating physical and genetic maps: from genomes to interaction networks. Nat. Rev. Genet. 2007, 8, 699-710.
    • (2007) Nat. Rev. Genet , vol.8 , pp. 699-710
    • Beyer, A.1    Bandyopadhyay, S.2    Ideker, T.3
  • 37
    • 11144293517 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling
    • Mawuenyega, K. G., Forst, C. V., Dobos, K. M., Belisle, J. T. et al., Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 2005, 16, 396-404.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 396-404
    • Mawuenyega, K.G.1    Forst, C.V.2    Dobos, K.M.3    Belisle, J.T.4
  • 38
    • 2342461648 scopus 로고    scopus 로고
    • Applicability of tandem affinity purification MudPIT to pathway proteomics in yeast
    • Graumann, J., Dunipace, L. A., Seol, J. H., McDonald, W. H. et al., Applicability of tandem affinity purification MudPIT to pathway proteomics in yeast. Mol. Cell. Proteomics 2004, 3, 226-237.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 226-237
    • Graumann, J.1    Dunipace, L.A.2    Seol, J.H.3    McDonald, W.H.4
  • 39
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E, Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 40
    • 0032875697 scopus 로고    scopus 로고
    • 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.
    • 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.
  • 41
    • 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. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 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
  • 42
    • 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
  • 43
    • 33748479920 scopus 로고    scopus 로고
    • Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages
    • Chertova, E., Chertov, O., Coren, L. V., Roser, J. D. et al., Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages. J. Virol. 2006, 80, 9039-9052.
    • (2006) J. Virol , vol.80 , pp. 9039-9052
    • Chertova, E.1    Chertov, O.2    Coren, L.V.3    Roser, J.D.4
  • 44
    • 33750705276 scopus 로고    scopus 로고
    • Proteomic analysis of urine in kidney transplant patients with BK virus nephropathy
    • Jahnukainen, T., Malehorn, D., Sun, M., Lyons-Weiler, J. et al., Proteomic analysis of urine in kidney transplant patients with BK virus nephropathy. J. Am. Soc. Nephrol. 2006, 17, 3248-3256.
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 3248-3256
    • Jahnukainen, T.1    Malehorn, D.2    Sun, M.3    Lyons-Weiler, J.4
  • 45
    • 33750576241 scopus 로고    scopus 로고
    • Viral proteomics: A promising approach for understanding JC virus tropism
    • Ravichandran, V., Major, E. O., Viral proteomics: a promising approach for understanding JC virus tropism. Proteomics 2006, 6, 5628-5636.
    • (2006) Proteomics , vol.6 , pp. 5628-5636
    • Ravichandran, V.1    Major, E.O.2
  • 46
    • 34848874473 scopus 로고    scopus 로고
    • Shotgun identification of structural proteome of shrimp white spot syndrome virus and iTRAQ differentiation of envelope and nucleocapsid subproteomes
    • in press
    • Li, Z., Lin, Q., Chen, J., Wu, J. L. et al., Shotgun identification of structural proteome of shrimp white spot syndrome virus and iTRAQ differentiation of envelope and nucleocapsid subproteomes. Mol. Cell. Proteomics 2007, (in press)
    • (2007) Mol. Cell. Proteomics
    • Li, Z.1    Lin, Q.2    Chen, J.3    Wu, J.L.4
  • 47
    • 33947525203 scopus 로고    scopus 로고
    • Proteomic study of the Bacillus subtilis ribosome: Finding of zinc-dependent replacement for ribosomal protein L31 paralogues
    • Nanamiya, H., Kawamura, F., Kosono, S., Proteomic study of the Bacillus subtilis ribosome: Finding of zinc-dependent replacement for ribosomal protein L31 paralogues. Gen. Appl. Microbiol. 2006, 52, 249-258.
    • (2006) Gen. Appl. Microbiol , vol.52 , pp. 249-258
    • Nanamiya, H.1    Kawamura, F.2    Kosono, S.3
  • 48
    • 34249808498 scopus 로고    scopus 로고
    • 2-DE proteomic analysis of the model cyanobacterium Anabaena variabilis
    • Barrios-Llerena, M. E., Reardon, K. F., Wright, P. C., 2-DE proteomic analysis of the model cyanobacterium Anabaena variabilis. Electrophoresis 2007, 28, 1624-1632.
    • (2007) Electrophoresis , vol.28 , pp. 1624-1632
    • Barrios-Llerena, M.E.1    Reardon, K.F.2    Wright, P.C.3
  • 49
    • 33947417316 scopus 로고    scopus 로고
    • Proteomic analysis of dimorphic transition in the phytopathogenic fungus Ustilago maydis
    • Bohmer, M., Colby, T., Bohmer, C., Brautigam, A. et al., Proteomic analysis of dimorphic transition in the phytopathogenic fungus Ustilago maydis. Proteomics 2007, 7, 675-685.
    • (2007) Proteomics , vol.7 , pp. 675-685
    • Bohmer, M.1    Colby, T.2    Bohmer, C.3    Brautigam, A.4
  • 50
    • 34248155865 scopus 로고    scopus 로고
    • Comparative proteomic analysis of B. cenocepacia using two-dimensional liquid separations coupled with mass spectrometry
    • Park, K. H., Lipuma, J. J., Lubman, D. M., Comparative proteomic analysis of B. cenocepacia using two-dimensional liquid separations coupled with mass spectrometry. Anal. Chim. Acta 2007, 592, 91-100.
    • (2007) Anal. Chim. Acta , vol.592 , pp. 91-100
    • Park, K.H.1    Lipuma, J.J.2    Lubman, D.M.3
  • 51
    • 0016833181 scopus 로고
    • New knowledge of chlamydiae and the diseases they cause
    • Grayston, J. T., Wang, S., New knowledge of chlamydiae and the diseases they cause. J. Infect. Dis. 1975, 132, 87-105.
    • (1975) J. Infect. Dis , vol.132 , pp. 87-105
    • Grayston, J.T.1    Wang, S.2
  • 52
    • 0026638792 scopus 로고
    • Chlamydia pneumoniae, strain TWAR pneumonia
    • Grayston, J. T., Chlamydia pneumoniae, strain TWAR pneumonia. Annu. Rev. Med. 1992, 43, 317-323.
    • (1992) Annu. Rev. Med , vol.43 , pp. 317-323
    • Grayston, J.T.1
  • 53
  • 54
    • 31844436891 scopus 로고    scopus 로고
    • Chlamydia and programmed cell death
    • Miyairi, I., Byrne, G. I., Chlamydia and programmed cell death. Curr. Opin. Microbiol. 2006, 9, 102-108.
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 102-108
    • Miyairi, I.1    Byrne, G.I.2
  • 55
    • 0034773537 scopus 로고    scopus 로고
    • Characterization of antiapoptotic activities of Chlamydia pneumoniae in human cells
    • Fischer, S. F., Schwarz, C., Vier, J., Hacker, G., Characterization of antiapoptotic activities of Chlamydia pneumoniae in human cells. Infect. Immun. 2001, 69, 7121-7129.
    • (2001) Infect. Immun , vol.69 , pp. 7121-7129
    • Fischer, S.F.1    Schwarz, C.2    Vier, J.3    Hacker, G.4
  • 56
    • 5444245799 scopus 로고    scopus 로고
    • Chlamydia inhibit host cell apoptosis by degradation of proapoptotic BH3-only proteins
    • Fischer, S. F., Vier, J., Kirschnek, S., Klos, A. et al., Chlamydia inhibit host cell apoptosis by degradation of proapoptotic BH3-only proteins. J. Exp. Med. 2004, 200, 905-916.
    • (2004) J. Exp. Med , vol.200 , pp. 905-916
    • Fischer, S.F.1    Vier, J.2    Kirschnek, S.3    Klos, A.4
  • 57
    • 0035078436 scopus 로고    scopus 로고
    • Persistent Chlamydia trachomatis infections resist apoptotic stimuli
    • Dean, D., Powers, V. C., Persistent Chlamydia trachomatis infections resist apoptotic stimuli.Infect. Immun, 2001, 69, 2442-2447.
    • (2001) Infect. Immun , vol.69 , pp. 2442-2447
    • Dean, D.1    Powers, V.C.2
  • 58
    • 0034725019 scopus 로고    scopus 로고
    • IgA1 protease from Neisseria gonorrhoeae inhibits TNFalpha-mediated apoptosis of human monocytic cells
    • Beck, S. C., Meyer, T. F., IgA1 protease from Neisseria gonorrhoeae inhibits TNFalpha-mediated apoptosis of human monocytic cells. FEBS Lett. 2000, 472, 287-292.
    • (2000) FEBS Lett , vol.472 , pp. 287-292
    • Beck, S.C.1    Meyer, T.F.2
  • 59
    • 0030965162 scopus 로고    scopus 로고
    • a matter of self control
    • Cell death induction by TNF
    • Wallach, D., Cell death induction by TNF: a matter of self control. Trends Biochem. Sci. 1997, 22, 107-109.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 107-109
    • Wallach, D.1
  • 60
    • 33846574355 scopus 로고    scopus 로고
    • Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems
    • Angot, A., Vergunst, A., Genin, S., Peeters, N., Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. PLoS Pathog. 2007, 3, e3.
    • (2007) PLoS Pathog , vol.3
    • Angot, A.1    Vergunst, A.2    Genin, S.3    Peeters, N.4
  • 62
    • 33747794347 scopus 로고    scopus 로고
    • Thiefes, A., Wolf, A., Doerrie, A., Grassl, G. A. et al., The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway. EMBO Rep. 2006, 7, 838-844.
    • Thiefes, A., Wolf, A., Doerrie, A., Grassl, G. A. et al., The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway. EMBO Rep. 2006, 7, 838-844.
  • 63
    • 27944471038 scopus 로고    scopus 로고
    • Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappa B activation
    • Zhou, H., Monack, D. M., Kayagaki, N., Wertz, I. et al., Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kappa B activation. J. Exp. Med. 2005, 202, 1327-1732.
    • (2005) J. Exp. Med , vol.202 , pp. 1327-1732
    • Zhou, H.1    Monack, D.M.2    Kayagaki, N.3    Wertz, I.4
  • 64
    • 0035039617 scopus 로고    scopus 로고
    • Quantitative pathology of inhalational anthrax I: Quantitative microscopic findings
    • Grinberg, L. M., Abramova, F.A., Yampolskaya, O. V., Walker, D. H. et al., Quantitative pathology of inhalational anthrax I: quantitative microscopic findings. Mod. Pathol. 2001, 14, 482-495.
    • (2001) Mod. Pathol , vol.14 , pp. 482-495
    • Grinberg, L.M.1    Abramova, F.A.2    Yampolskaya, O.V.3    Walker, D.H.4
  • 66
    • 4444350477 scopus 로고    scopus 로고
    • Targeting of Bacillus anthracis interaction factors for human macrophages using two-dimensional gel electrophoresis
    • Seo, G. M., Kim, S. J., Kim, J. C., Nam, D. H. et al., Targeting of Bacillus anthracis interaction factors for human macrophages using two-dimensional gel electrophoresis. Biochem. Biophys. Res. Commun. 2004, 322, 854-859.
    • (2004) Biochem. Biophys. Res. Commun , vol.322 , pp. 854-859
    • Seo, G.M.1    Kim, S.J.2    Kim, J.C.3    Nam, D.H.4
  • 67
    • 33748532143 scopus 로고    scopus 로고
    • Proteomic analyses of murine macrophages treated with Bacillus anthracis lethal toxin
    • Sapra, R., Gaucher, S. P., Lachmann, J. S., Buffleben, G. M. et al., Proteomic analyses of murine macrophages treated with Bacillus anthracis lethal toxin. Microb. Pathog. 2006, 41, 157-167.
    • (2006) Microb. Pathog , vol.41 , pp. 157-167
    • Sapra, R.1    Gaucher, S.P.2    Lachmann, J.S.3    Buffleben, G.M.4
  • 68
    • 33646241299 scopus 로고    scopus 로고
    • Proteomics study of anthrax lethal toxin-treated murine macrophages
    • Kuhn, J. F., Hoerth, P., Hoehn, S. T., Preckel, T., Tomer, K. B., Proteomics study of anthrax lethal toxin-treated murine macrophages. Electrophoresis 2006, 7, 1584-1597.
    • (2006) Electrophoresis , vol.7 , pp. 1584-1597
    • Kuhn, J.F.1    Hoerth, P.2    Hoehn, S.T.3    Preckel, T.4    Tomer, K.B.5
  • 69
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem, R., Hakem, A., Duncan, G. S., Henderson, J. T. et al., Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 1998, 94, 339-352.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3    Henderson, J.T.4
  • 70
    • 34248650464 scopus 로고    scopus 로고
    • Proteomic analysis of up-regulated proteins in human promonocyte cells expressing severe acute respiratory syndrome coronavirus 3C-like protease
    • Lai, C. C., Jou, M. J., Huang, S. Y., Li, S. W. et al., Proteomic analysis of up-regulated proteins in human promonocyte cells expressing severe acute respiratory syndrome coronavirus 3C-like protease. Proteomics 2007, 7, 1446-1460.
    • (2007) Proteomics , vol.7 , pp. 1446-1460
    • Lai, C.C.1    Jou, M.J.2    Huang, S.Y.3    Li, S.W.4
  • 71
    • 33645089410 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome Coronavirus 3C-like protease-induced apoptosis
    • Lin, C. W., Lin, K. H., Hsieh, T. H., Shiu, S. Y., Li, J. Y., Severe acute respiratory syndrome Coronavirus 3C-like protease-induced apoptosis. FEMS Immunol. Med. Microbiol. 2006, 46, 375-380.
    • (2006) FEMS Immunol. Med. Microbiol , vol.46 , pp. 375-380
    • Lin, C.W.1    Lin, K.H.2    Hsieh, T.H.3    Shiu, S.Y.4    Li, J.Y.5
  • 72
    • 2942756226 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway
    • Roos-Mattjus, P., Sistonen, L., The ubiquitin-proteasome pathway. Ann. Med. 2004, 36, 285-295.
    • (2004) Ann. Med , vol.36 , pp. 285-295
    • Roos-Mattjus, P.1    Sistonen, L.2
  • 73
    • 2142857233 scopus 로고    scopus 로고
    • Preparation and characterization of recombinant murine p65/L-plastin expressed in Escherichia coli and high-titer antibodies against the protein
    • Shinomiya, H., Nagai, K., Hirata, H., Kobayashi, N. et al., Preparation and characterization of recombinant murine p65/L-plastin expressed in Escherichia coli and high-titer antibodies against the protein. Biosci. Biotechnol. Biochem. 2003, 67, 1368-1375.
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 1368-1375
    • Shinomiya, H.1    Nagai, K.2    Hirata, H.3    Kobayashi, N.4
  • 74
    • 0037452070 scopus 로고    scopus 로고
    • Microbial pathogenesis and cytoskeletal function
    • Gruenheid, S., Finlay, B. B., Microbial pathogenesis and cytoskeletal function. Nature 2003, 422, 775-781.
    • (2003) Nature , vol.422 , pp. 775-781
    • Gruenheid, S.1    Finlay, B.B.2
  • 75
    • 10744221155 scopus 로고    scopus 로고
    • Functional analysis of the cag pathogenicity island in Helicobacter pylori isolates from patients with gastritis, peptic ulcer, and gastric cancer
    • Backen, S., Schwarz, T., Miehlke, S., Kirsch, C. et al., Functional analysis of the cag pathogenicity island in Helicobacter pylori isolates from patients with gastritis, peptic ulcer, and gastric cancer. Infect. Immun. 2004, 72, 1043-1056.
    • (2004) Infect. Immun , vol.72 , pp. 1043-1056
    • Backen, S.1    Schwarz, T.2    Miehlke, S.3    Kirsch, C.4
  • 76
    • 0038070120 scopus 로고    scopus 로고
    • Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility
    • Fischer, R. S., Fritz-Six, K. L., Fowler, V. M., Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility. J. Cell Biol. 2003, 161, 371-380.
    • (2003) J. Cell Biol , vol.161 , pp. 371-380
    • Fischer, R.S.1    Fritz-Six, K.L.2    Fowler, V.M.3
  • 77
    • 0037160062 scopus 로고    scopus 로고
    • Activation of pyk2/related focal adhesion tyrosine kinase and focal adhesion kinase in cardiac remodeling
    • Melendez, J., Welch, S., Schaefer, E., Moravec, C. S., Activation of pyk2/related focal adhesion tyrosine kinase and focal adhesion kinase in cardiac remodeling. J. Biol. Chem. 2002, 277, 45203-45210.
    • (2002) J. Biol. Chem , vol.277 , pp. 45203-45210
    • Melendez, J.1    Welch, S.2    Schaefer, E.3    Moravec, C.S.4
  • 78
    • 0037415684 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation
    • Selbach, M., Moese, S., Hurwitz, R., Hauck, C. R. et al., The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation. EMBO J. 2003, 22, 515-528.
    • (2003) EMBO J , vol.22 , pp. 515-528
    • Selbach, M.1    Moese, S.2    Hurwitz, R.3    Hauck, C.R.4
  • 79
    • 2542635813 scopus 로고    scopus 로고
    • Helicobacter pylori induces AGS cell motility and elongation via independent signaling pathways
    • Moese, S., Selbach, M., Kwok, T., Brinkmann, V. et al., Helicobacter pylori induces AGS cell motility and elongation via independent signaling pathways. Infect. Immun. 2004, 72, 3646-3649.
    • (2004) Infect. Immun , vol.72 , pp. 3646-3649
    • Moese, S.1    Selbach, M.2    Kwok, T.3    Brinkmann, V.4
  • 80
    • 18044369328 scopus 로고    scopus 로고
    • Gene expression and protein profiling of AGS gastric epithelial cells upon infection with Helicobacter pylori
    • Backert, S., Gressmann, H., Kwok, T., Zimny-Arndt, U. et al., Gene expression and protein profiling of AGS gastric epithelial cells upon infection with Helicobacter pylori. Proteomics 2005, 5, 3902-3918.
    • (2005) Proteomics , vol.5 , pp. 3902-3918
    • Backert, S.1    Gressmann, H.2    Kwok, T.3    Zimny-Arndt, U.4
  • 81
    • 0036607439 scopus 로고    scopus 로고
    • Cellular hijacking: A common strategy for microbial infection
    • Kahn, R. A., Fu, H., Roy, C. R., Cellular hijacking: a common strategy for microbial infection. Trends Biochem. Sci. 2002, 27, 308-314.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 308-314
    • Kahn, R.A.1    Fu, H.2    Roy, C.R.3
  • 82
    • 0033588919 scopus 로고    scopus 로고
    • Listeria monocytogenes exploits normal host cell processes to spread from cell to cell
    • Robbins, J. R., Barth, A. I., Marquis, H., de Hostos, E.L. et al., Listeria monocytogenes exploits normal host cell processes to spread from cell to cell. J. Cell. Biol. 1999, 146, 1333-1350.
    • (1999) J. Cell. Biol , vol.146 , pp. 1333-1350
    • Robbins, J.R.1    Barth, A.I.2    Marquis, H.3    de Hostos, E.L.4
  • 83
    • 0026515440 scopus 로고    scopus 로고
    • Kocks, C., Gouin, E., Tabouret, M., Berche, P. et al., L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 1992, 68, 521-531.
    • Kocks, C., Gouin, E., Tabouret, M., Berche, P. et al., L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 1992, 68, 521-531.
  • 85
    • 33644863314 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection
    • Leong, W. F., Chow, V. T., Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006, 8, 565-580.
    • (2006) Cell Microbiol , vol.8 , pp. 565-580
    • Leong, W.F.1    Chow, V.T.2
  • 86
    • 0031745447 scopus 로고    scopus 로고
    • The stathmin phosphoprotein family: Intracellular localization and effects on the microtubule network
    • Gavet, O., Ozon, S., Manceau, V., Lawler, S. et al., The stathmin phosphoprotein family: intracellular localization and effects on the microtubule network. J. Cell Sci. 1998, 111, 3333-3346.
    • (1998) J. Cell Sci , vol.111 , pp. 3333-3346
    • Gavet, O.1    Ozon, S.2    Manceau, V.3    Lawler, S.4
  • 87
    • 0035104426 scopus 로고    scopus 로고
    • Evidence for the relation of herpes simplex virus type 1 to Down syndrome and Alzheimer's disease
    • Cheon, M. S., Bajo, M., Gulesserian, T., Cairns, N., Lubec, G., Evidence for the relation of herpes simplex virus type 1 to Down syndrome and Alzheimer's disease. Electrophoresis 2001, 22, 445-448.
    • (2001) Electrophoresis , vol.22 , pp. 445-448
    • Cheon, M.S.1    Bajo, M.2    Gulesserian, T.3    Cairns, N.4    Lubec, G.5
  • 88
    • 0033017374 scopus 로고    scopus 로고
    • Enteroviral protease 2A cleaves dystrophin: Evidence of cytoskeletal disruption in an acquired cardiomyopathy
    • Badorff, C., Lee, G. H., Lamphear, B. J., Martone, M. E., et al., Enteroviral protease 2A cleaves dystrophin: evidence of cytoskeletal disruption in an acquired cardiomyopathy. Nat. Med. 1999, 5, 320-326.
    • (1999) Nat. Med , vol.5 , pp. 320-326
    • Badorff, C.1    Lee, G.H.2    Lamphear, B.J.3    Martone, M.E.4
  • 89
    • 33747358795 scopus 로고    scopus 로고
    • Proteome alterations in human host cells infected with coxsackievirus B3
    • Rassmann, A., Henke, A., Zobawa, M., Carlsohn, M. et al., Proteome alterations in human host cells infected with coxsackievirus B3. J. Gen. Virol. 2006, 87, 2631-2638.
    • (2006) J. Gen. Virol , vol.87 , pp. 2631-2638
    • Rassmann, A.1    Henke, A.2    Zobawa, M.3    Carlsohn, M.4
  • 90
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • Burke, B., Stewart, C. L., Life at the edge: the nuclear envelope and human disease. Nat. Rev. Mol. Cell Biol. 2002, 3, 575-585.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 91
    • 0029943398 scopus 로고    scopus 로고
    • Recombinant human immunodeficiency virus type 1 genomes with tat unconstrained by overlapping reading frames reveal residues in Tat important for replication in tissue culture
    • Neuveut, C., Jeang, K. T., Recombinant human immunodeficiency virus type 1 genomes with tat unconstrained by overlapping reading frames reveal residues in Tat important for replication in tissue culture. J. Virol. 1996, 70, 5572-5581.
    • (1996) J. Virol , vol.70 , pp. 5572-5581
    • Neuveut, C.1    Jeang, K.T.2
  • 92
    • 33947433457 scopus 로고    scopus 로고
    • Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression
    • Coiras, M., Camafeita, E., Urena, T., Lopez, J. A. et al., Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression. Proteomics 2006, 6, S63-3.
    • (2006) Proteomics , vol.6
    • Coiras, M.1    Camafeita, E.2    Urena, T.3    Lopez, J.A.4
  • 93
    • 12244304872 scopus 로고    scopus 로고
    • HIV-1 Tat targets microtubules to induce apoptosis, a process promoted by the pro-apoptotic Bcl-2 relative Bim
    • Chen, D., Wang, M., Zhou, S., Zhou, Q., HIV-1 Tat targets microtubules to induce apoptosis, a process promoted by the pro-apoptotic Bcl-2 relative Bim. EMBO J. 2002, 21, 6801-6810.
    • (2002) EMBO J , vol.21 , pp. 6801-6810
    • Chen, D.1    Wang, M.2    Zhou, S.3    Zhou, Q.4
  • 94
    • 0017594885 scopus 로고
    • Persistence of Toxoplasma gondii in the tissues of chronically infected cats
    • Dubey, J. P., Persistence of Toxoplasma gondii in the tissues of chronically infected cats. J. Parasitol. 1977, 63, 156-157.
    • (1977) J. Parasitol , vol.63 , pp. 156-157
    • Dubey, J.P.1
  • 96
    • 0033103170 scopus 로고    scopus 로고
    • Armed and dangerous: Toxoplasma gondii uses an arsenal of secretory proteins to infect host cells
    • Carruthers, V. B., Armed and dangerous: Toxoplasma gondii uses an arsenal of secretory proteins to infect host cells. Parasitol. Int. 1999, 48, 1-10.
    • (1999) Parasitol. Int , vol.48 , pp. 1-10
    • Carruthers, V.B.1
  • 97
    • 0036372942 scopus 로고    scopus 로고
    • The glideosome': A dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii
    • Opitz, C., Soldati, D., 'The glideosome': a dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii. Mol. Microbiol. 2002, 45, 597-604.
    • (2002) Mol. Microbiol , vol.45 , pp. 597-604
    • Opitz, C.1    Soldati, D.2
  • 98
    • 26644451857 scopus 로고    scopus 로고
    • Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interactions in Toxoplasma gondii
    • Bradley, P. J., Ward, C., Cheng, S. J., Alexander, D. L. et al., Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interactions in Toxoplasma gondii. J. Biol. Chem. 2005, 280, 34245-34258.
    • (2005) J. Biol. Chem , vol.280 , pp. 34245-34258
    • Bradley, P.J.1    Ward, C.2    Cheng, S.J.3    Alexander, D.L.4
  • 99
    • 34250891237 scopus 로고    scopus 로고
    • Coxsackievirus b3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I
    • Cornell, C. T., Kiosses, W. B., Harkins, S., Whitton, J. L., Coxsackievirus b3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. J. Virol. 2007, 81, 6785-6797.
    • (2007) J. Virol , vol.81 , pp. 6785-6797
    • Cornell, C.T.1    Kiosses, W.B.2    Harkins, S.3    Whitton, J.L.4
  • 101
    • 0034877005 scopus 로고    scopus 로고
    • Poliovirus 3A protein limits interleukin-6 (IL-6), IL-8, and beta interferon secretion during viral infection
    • Dodd, D. A., Giddings, T. H. Jr, Kirkegaard, K., Poliovirus 3A protein limits interleukin-6 (IL-6), IL-8, and beta interferon secretion during viral infection. J. Virol. 2001, 75, 8158-8165.
    • (2001) J. Virol , vol.75 , pp. 8158-8165
    • Dodd, D.A.1    Giddings Jr, T.H.2    Kirkegaard, K.3
  • 102
    • 0033776709 scopus 로고    scopus 로고
    • HIV-1 Nef protein binds to the cellular protein PACS-1 to down-regulate class I major histocompatibility complexes
    • Piguet, V., Wan, L., Borel, C., Mangasarian, A. et al., HIV-1 Nef protein binds to the cellular protein PACS-1 to down-regulate class I major histocompatibility complexes. Nat. Cell Biol. 2000, 2, 163-197.
    • (2000) Nat. Cell Biol , vol.2 , pp. 163-197
    • Piguet, V.1    Wan, L.2    Borel, C.3    Mangasarian, A.4
  • 103
    • 0029875421 scopus 로고    scopus 로고
    • Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein
    • Schwartz, O., Maréchal, V., Le Gall, S., Lemonnier, F., Heard, J. M., Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nature Med. 1996, 2, 338-342.
    • (1996) Nature Med , vol.2 , pp. 338-342
    • Schwartz, O.1    Maréchal, V.2    Le Gall, S.3    Lemonnier, F.4    Heard, J.M.5
  • 104
    • 0032563306 scopus 로고    scopus 로고
    • PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization
    • Wan, L., Molloy, S. S., Thomas, L., Liu, G. et al., PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization. Cell 1998, 94, 205-216.
    • (1998) Cell , vol.94 , pp. 205-216
    • Wan, L.1    Molloy, S.S.2    Thomas, L.3    Liu, G.4
  • 105
    • 0037074008 scopus 로고    scopus 로고
    • HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway
    • Blagoveshchenskaya, A. D., Thomas, L., Feliciangeli, S. F., Hung, C. H., Thomas, G., HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway. Cell 2002, 111, 853-866.
    • (2002) Cell , vol.111 , pp. 853-866
    • Blagoveshchenskaya, A.D.1    Thomas, L.2    Feliciangeli, S.F.3    Hung, C.H.4    Thomas, G.5
  • 106
    • 0031575530 scopus 로고    scopus 로고
    • Binding of HIV-1 to its receptor induces tyrosine phosphorylation of several CD4-associated proteins, including the phosphatidylinositol 3-kinase
    • Briand, G., Barbeau, B., Tremblay, M., Binding of HIV-1 to its receptor induces tyrosine phosphorylation of several CD4-associated proteins, including the phosphatidylinositol 3-kinase. Virology 1997, 228, 171-179.
    • (1997) Virology , vol.228 , pp. 171-179
    • Briand, G.1    Barbeau, B.2    Tremblay, M.3
  • 107
    • 0030007126 scopus 로고    scopus 로고
    • HIV induces activation of phosphatidylinositol 4-kinase and mitogen-activated protein kinase by interacting with T cell CD4 surface molecules
    • Schmid-Antomarchi, H., Benkirane, M., Breittmayer, V., Husson, H. et al., HIV induces activation of phosphatidylinositol 4-kinase and mitogen-activated protein kinase by interacting with T cell CD4 surface molecules. Eur. J. Immunol. 1996, 26, 717-720.
    • (1996) Eur. J. Immunol , vol.26 , pp. 717-720
    • Schmid-Antomarchi, H.1    Benkirane, M.2    Breittmayer, V.3    Husson, H.4
  • 108
    • 0028176569 scopus 로고
    • Association of p56lck with the cytoplasmic domain of CD4 modulates HIV-1 expression
    • Tremblay, M., Meloche, S., Gratton, S., Wainberg, M. A., Sekaly, R. P., Association of p56lck with the cytoplasmic domain of CD4 modulates HIV-1 expression. EMBO J. 1994, 13, 774-783.
    • (1994) EMBO J , vol.13 , pp. 774-783
    • Tremblay, M.1    Meloche, S.2    Gratton, S.3    Wainberg, M.A.4    Sekaly, R.P.5
  • 109
    • 0029949810 scopus 로고    scopus 로고
    • Repression of human immunodeficiency virus type 1 long terminal repeat-driven gene expression by binding of the virus to its primary cellular receptor, the CD4 molecule
    • Berube, P., Barbeau, B., Cantin, R., Sekaly, R. P., Tremblay, M., Repression of human immunodeficiency virus type 1 long terminal repeat-driven gene expression by binding of the virus to its primary cellular receptor, the CD4 molecule. J. Virol. 1996, 70, 4009-4016.
    • (1996) J. Virol , vol.70 , pp. 4009-4016
    • Berube, P.1    Barbeau, B.2    Cantin, R.3    Sekaly, R.P.4    Tremblay, M.5
  • 110
    • 0031812844 scopus 로고    scopus 로고
    • The acquisition of host-encoded proteins by nascent HIV-1
    • Tremblay, M. J., Fortin, J. F., Cantin, R., The acquisition of host-encoded proteins by nascent HIV-1. Immunol. Today 1998, 19, 346-351.
    • (1998) Immunol. Today , vol.19 , pp. 346-351
    • Tremblay, M.J.1    Fortin, J.F.2    Cantin, R.3
  • 111
    • 33846014643 scopus 로고    scopus 로고
    • Modification of host lipid raft proteome upon hepatitis C virus replication
    • Mannova, P., Fang, R., Wang, H., Deng, B. et al., Modification of host lipid raft proteome upon hepatitis C virus replication. Mol. Cell. Proteomics 2006, 5, 2319-2325.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2319-2325
    • Mannova, P.1    Fang, R.2    Wang, H.3    Deng, B.4
  • 112
    • 8444243363 scopus 로고    scopus 로고
    • Targeting Rab GTPases to distinct membrane compartments
    • Pfeffer, S., Aivazian, D., Targeting Rab GTPases to distinct membrane compartments. Nat. Rev Mol. Cell. Biol. 2004, 5, 886-889.
    • (2004) Nat. Rev Mol. Cell. Biol , vol.5 , pp. 886-889
    • Pfeffer, S.1    Aivazian, D.2
  • 113
    • 10944244704 scopus 로고    scopus 로고
    • Rho signalling at a glance
    • Schwartz, M., Rho signalling at a glance. J. Cell. Sci. 2004, 117, 5457-5458.
    • (2004) J. Cell. Sci , vol.117 , pp. 5457-5458
    • Schwartz, M.1
  • 114
    • 21644460984 scopus 로고    scopus 로고
    • Activation of the N-Ras-PI3K-Akt-mTOR pathway by hepatitis C virus: Control of cell survival and viral replication
    • Mannová, P., Beretta, L., Activation of the N-Ras-PI3K-Akt-mTOR pathway by hepatitis C virus: control of cell survival and viral replication. J. Virol. 2005, 79, 8742-8749.
    • (2005) J. Virol , vol.79 , pp. 8742-8749
    • Mannová, P.1    Beretta, L.2
  • 115
    • 5644226060 scopus 로고    scopus 로고
    • Continued proteomic analysis of Mycobacterium leprae subcellular fractions
    • Marques, M. A., Espinosa, B. J., Xavier da Silveira, E. K., Pessolani, M. C. et al., Continued proteomic analysis of Mycobacterium leprae subcellular fractions. Proteomics 2004, 4, 2942-2953.
    • (2004) Proteomics , vol.4 , pp. 2942-2953
    • Marques, M.A.1    Espinosa, B.J.2    Xavier da Silveira, E.K.3    Pessolani, M.C.4
  • 116
    • 0003492394 scopus 로고
    • Bloom, B.R, Ed, American Society for Microbiology Press, Washington
    • Bloom, B.R. (Ed.), in: Tuberculosis: Pathogenesis, Protection and Control. American Society for Microbiology Press, Washington 1994, pp. 353-385.
    • (1994) Tuberculosis: Pathogenesis, Protection and Control , pp. 353-385
  • 117
    • 0035928765 scopus 로고    scopus 로고
    • Hepatitis C virus core protein: Intriguing properties and functional relevance
    • Ray, R. B., Ray, R.Hepatitis C virus core protein: intriguing properties and functional relevance. FEMS Microbiol. Lett. 2001, 202, 149-156.
    • (2001) FEMS Microbiol. Lett , vol.202 , pp. 149-156
    • Ray, R.B.1    Ray, R.2
  • 118
    • 33745756902 scopus 로고    scopus 로고
    • Proteomic profiling of lipid droplet proteins in hepatoma cell lines expressing hepatitis C virus core protein
    • Sato, S., Fukasawa, M., Yamakawa, Y., Natsume, T. et al., Proteomic profiling of lipid droplet proteins in hepatoma cell lines expressing hepatitis C virus core protein. J. Biochem. 2006, 139, 921-930.
    • (2006) J. Biochem , vol.139 , pp. 921-930
    • Sato, S.1    Fukasawa, M.2    Yamakawa, Y.3    Natsume, T.4
  • 119
    • 4744352786 scopus 로고    scopus 로고
    • Management and resistance in wheat and barley to Fusarium head blight
    • Bai, G., Shaner, G., Management and resistance in wheat and barley to Fusarium head blight. Annu. Rev. Phytopathol. 2004, 42, 135-161.
    • (2004) Annu. Rev. Phytopathol , vol.42 , pp. 135-161
    • Bai, G.1    Shaner, G.2
  • 120
    • 0036938936 scopus 로고    scopus 로고
    • Molecular mapping of QTLs for Fusarium head blight resistance in spring wheat. I. Resistance to fungal spread (Type II resistance)
    • Buerstmayr, H., Lemmens, M., Hartl, L., Doldi, L. et al., Molecular mapping of QTLs for Fusarium head blight resistance in spring wheat. I. Resistance to fungal spread (Type II resistance). Theor. Appl. Genet. 2002, 104, 84-91.
    • (2002) Theor. Appl. Genet , vol.104 , pp. 84-91
    • Buerstmayr, H.1    Lemmens, M.2    Hartl, L.3    Doldi, L.4
  • 121
    • 33748344060 scopus 로고    scopus 로고
    • Identification of differentially regulated proteins in response to a compatible interaction between the pathogen Fusarium graminearum and its host, Triticum aestivum
    • Zhou, W., Eudes, F., Laroche, A., Identification of differentially regulated proteins in response to a compatible interaction between the pathogen Fusarium graminearum and its host, Triticum aestivum. Proteomics 2006, 6, 4599-4609.
    • (2006) Proteomics , vol.6 , pp. 4599-4609
    • Zhou, W.1    Eudes, F.2    Laroche, A.3
  • 122
    • 33847421368 scopus 로고    scopus 로고
    • Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches
    • Mayer, D., Molawi, K., Martínez-Sobrido, L., Ghanem, A. et al., Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches. J. Proteome Res. 2007, 6, 672-682.
    • (2007) J. Proteome Res , vol.6 , pp. 672-682
    • Mayer, D.1    Molawi, K.2    Martínez-Sobrido, L.3    Ghanem, A.4
  • 123
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang, P., Palese, P., O'Neil, R. E., The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J. Virol. 1997, 71, 1850-1856.
    • (1997) J. Virol , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neil, R.E.3
  • 124
    • 0032981158 scopus 로고    scopus 로고
    • Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments
    • Digard, P., Elton, D., Bishop, K., Medcalf, E., et al., Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments. J. Virol. 1999, 73, 2222-2231.
    • (1999) J. Virol , vol.73 , pp. 2222-2231
    • Digard, P.1    Elton, D.2    Bishop, K.3    Medcalf, E.4
  • 125
    • 0034892686 scopus 로고    scopus 로고
    • PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators
    • Huarte, M., Sanz-Ezquerro, J. J., Roncal, F., Ortin, J., Nieto, A., PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators. J. Virol. 2001, 75, 8597-8604.
    • (2001) J. Virol , vol.75 , pp. 8597-8604
    • Huarte, M.1    Sanz-Ezquerro, J.J.2    Roncal, F.3    Ortin, J.4    Nieto, A.5
  • 126
    • 0346003805 scopus 로고    scopus 로고
    • Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis
    • Momose, F., Naito, T., Yano, K., Sugimoto, S. et al., Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis. J. Biol. Chem. 2002, 277, 45306-45314.
    • (2002) J. Biol. Chem , vol.277 , pp. 45306-45314
    • Momose, F.1    Naito, T.2    Yano, K.3    Sugimoto, S.4
  • 127
    • 17444430403 scopus 로고    scopus 로고
    • Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II
    • Engelhardt, O. G., Smith, M., Fodor, E., Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II. J. Virol. 2005, 79, 5812-5818.
    • (2005) J. Virol , vol.79 , pp. 5812-5818
    • Engelhardt, O.G.1    Smith, M.2    Fodor, E.3
  • 128
    • 2442653990 scopus 로고    scopus 로고
    • Taylor, T. J., Knipe, D. M., Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 2004, 78, 5856-5866.
    • Taylor, T. J., Knipe, D. M., Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 2004, 78, 5856-5866.
  • 129
    • 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
  • 130
    • 13444266131 scopus 로고    scopus 로고
    • The role of peptidoglycan in pathogenesis
    • Boneca, I. G., The role of peptidoglycan in pathogenesis. Curr. Opin. Microbiol. 2005, 8, 46-53.
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 46-53
    • Boneca, I.G.1
  • 131
    • 0032995471 scopus 로고    scopus 로고
    • Molecular and cellular biology of pneumococcal infection
    • Tuomanen, E., Molecular and cellular biology of pneumococcal infection. Curr. Opin. Microbiol. 1999, 2, 35-39.
    • (1999) Curr. Opin. Microbiol , vol.2 , pp. 35-39
    • Tuomanen, E.1
  • 132
    • 0033852411 scopus 로고    scopus 로고
    • Regulation of growth inhibition at high temperature, autolysis, transformation and adherence in Streptococcus pneumoniae by clpC
    • Charpentier, E., Novak, R., Tuomanen, E., Regulation of growth inhibition at high temperature, autolysis, transformation and adherence in Streptococcus pneumoniae by clpC. Mol. Microbiol. 2000, 37, 717-726.
    • (2000) Mol. Microbiol , vol.37 , pp. 717-726
    • Charpentier, E.1    Novak, R.2    Tuomanen, E.3
  • 133
    • 33845395519 scopus 로고    scopus 로고
    • The effect of protein expression of Streptococcus pneumoniae by blood
    • Bae, S. M., Yeon, S. M., Kim, T. S., Lee, K. J., The effect of protein expression of Streptococcus pneumoniae by blood. J. Biochem. Mol. Biol. 2006, 39, 703-708.
    • (2006) J. Biochem. Mol. Biol , vol.39 , pp. 703-708
    • Bae, S.M.1    Yeon, S.M.2    Kim, T.S.3    Lee, K.J.4
  • 134
    • 33644543756 scopus 로고    scopus 로고
    • Proteomic analysis of growth phase-dependent proteins of Streptococcus pneumoniae
    • Lee, K. J., Bae, S. M., Lee, M. R., Yeon, S. M. et al., Proteomic analysis of growth phase-dependent proteins of Streptococcus pneumoniae. Proteomics 2006, 6, 1274-1282.
    • (2006) Proteomics , vol.6 , pp. 1274-1282
    • Lee, K.J.1    Bae, S.M.2    Lee, M.R.3    Yeon, S.M.4
  • 135
    • 33750587190 scopus 로고    scopus 로고
    • Proteomic analysis of protein expression in Streptococcus pneumoniae in response to temperature shift
    • Lee, M. R., Bae, S. M., Kim, T. S., Lee, K. J., Proteomic analysis of protein expression in Streptococcus pneumoniae in response to temperature shift. J. Microbiol. 2006, 44, 375-382.
    • (2006) J. Microbiol , vol.44 , pp. 375-382
    • Lee, M.R.1    Bae, S.M.2    Kim, T.S.3    Lee, K.J.4
  • 136
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., Scott, J. D., Signaling through scaffold, anchoring, and adaptor proteins. Science 1997, 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 137
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: Identification of a novel protein, Frigg, as a protein kinase A substrate
    • Gronborg, M., Kristiansen, T. Z., Stensballe, A., Andersen, J. S., et al., A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate. Mol. Cell. Proteomics 2002, 1, 517-527.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 517-527
    • Gronborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4
  • 138
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J. et al., Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 2002, 20, 301-305.
    • (2002) Nat. Biotechnol , vol.20 , pp. 301-305
    • Ficarro, S.B.1    McCleland, M.L.2    Stukenberg, P.T.3    Burke, D.J.4
  • 139
    • 0037302253 scopus 로고    scopus 로고
    • Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication
    • Law, L. M. J., Everitt, J. C., Beatch, M. D., Holmes, C. F. B., Hobman, T. C., Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication. J. Virol. 2003, 77, 1764-1771.
    • (2003) J. Virol , vol.77 , pp. 1764-1771
    • Law, L.M.J.1    Everitt, J.C.2    Beatch, M.D.3    Holmes, C.F.B.4    Hobman, T.C.5
  • 140
    • 0030731422 scopus 로고    scopus 로고
    • Nuclear import and export of influenza virus nucleoprotein
    • Neumann, G., Castrucci, M. R., Kawaoka, Y., Nuclear import and export of influenza virus nucleoprotein. J. Virol. 1997, 71, 9690-9700.
    • (1997) J. Virol , vol.71 , pp. 9690-9700
    • Neumann, G.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 141
    • 0036229472 scopus 로고    scopus 로고
    • Both viral transcription and replication are reduced when the rabies virus nucleoprotein is not phosphorylated
    • Wu, X., Gong, X., Foley, H. D., Schnell, M. J., Fu, Z. F., Both viral transcription and replication are reduced when the rabies virus nucleoprotein is not phosphorylated. J. Virol. 2002, 76, 4153-4161.
    • (2002) J. Virol , vol.76 , pp. 4153-4161
    • Wu, X.1    Gong, X.2    Foley, H.D.3    Schnell, M.J.4    Fu, Z.F.5
  • 143
    • 23044516385 scopus 로고    scopus 로고
    • Phosphorylation and subcellular localization of transmissible gastroenteritis virus nucleocapsid protein in infected cells
    • Calvo, E., Escors, D., López, J. A., González, J. M. et al., Phosphorylation and subcellular localization of transmissible gastroenteritis virus nucleocapsid protein in infected cells. J. Gen. Virol. 2005, 86, 2255-2267.
    • (2005) J. Gen. Virol , vol.86 , pp. 2255-2267
    • Calvo, E.1    Escors, D.2    López, J.A.3    González, J.M.4
  • 145
    • 33751421061 scopus 로고    scopus 로고
    • Phosphorylation of human respiratory syncytial virus P protein at threonine 108 controls its interaction with the M2-1 protein in the viral RNA polymerase complex
    • Asenjo, A., Calvo, E., Villanueva, N., Phosphorylation of human respiratory syncytial virus P protein at threonine 108 controls its interaction with the M2-1 protein in the viral RNA polymerase complex. J. Gen. Virol. 2006, 87, 3637-3642.
    • (2006) J. Gen. Virol , vol.87 , pp. 3637-3642
    • Asenjo, A.1    Calvo, E.2    Villanueva, N.3
  • 146
    • 0038631572 scopus 로고    scopus 로고
    • Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome
    • Pitarch, A., Sánchez, M., Nombela, C., Gil, C., Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome. Mol. Cell. Proteomics 2002, 1, 967-982.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 967-982
    • Pitarch, A.1    Sánchez, M.2    Nombela, C.3    Gil, C.4
  • 147
    • 5644226058 scopus 로고    scopus 로고
    • Comparative proteome analysis of cellular proteins extracted from highly virulent Francisella tularensis ssp. tularensis and less virulent F. tularensis ssp. holarctica and F. tularensis ssp
    • Hubalek, M., Hernychova, L., Brychta, M., Lenco, J. et al., Comparative proteome analysis of cellular proteins extracted from highly virulent Francisella tularensis ssp. tularensis and less virulent F. tularensis ssp. holarctica and F. tularensis ssp. Mediaasiatica. Proteomics 2004, 4, 3048-3060.
    • (2004) Mediaasiatica. Proteomics , vol.4 , pp. 3048-3060
    • Hubalek, M.1    Hernychova, L.2    Brychta, M.3    Lenco, J.4
  • 148
    • 33847617561 scopus 로고    scopus 로고
    • Proteomics analysis of the Francisella tularensis LVS response to iron restriction: Induction of the F. tularensis pathogenicity island proteins IgIABC
    • Lenco, J., Hubalek, M., Larsson, P., Fucikova, A. et al., Proteomics analysis of the Francisella tularensis LVS response to iron restriction: induction of the F. tularensis pathogenicity island proteins IgIABC. FEMS Microbiol. Lett. 2007, 269, 11-21.
    • (2007) FEMS Microbiol. Lett , vol.269 , pp. 11-21
    • Lenco, J.1    Hubalek, M.2    Larsson, P.3    Fucikova, A.4
  • 149
    • 33845474710 scopus 로고    scopus 로고
    • Expression of Pseudomonas aeruginosa toxin ExoS effectively induces apoptosis in host cells
    • Jia, J., Wang, Y., Zhou, L., Jin, S., Expression of Pseudomonas aeruginosa toxin ExoS effectively induces apoptosis in host cells. Infect. Immun. 2006, 74, 6557-6570.
    • (2006) Infect. Immun , vol.74 , pp. 6557-6570
    • Jia, J.1    Wang, Y.2    Zhou, L.3    Jin, S.4
  • 150
    • 17244376424 scopus 로고    scopus 로고
    • Proteomic characterization of Yersinia pestis virulence
    • Chromy, B. A., Choi, M. W., Murphy, G. A., Gonzales, A. D. et al., Proteomic characterization of Yersinia pestis virulence. J. Bacteriol. 2005, 187, 8172-8180.
    • (2005) J. Bacteriol , vol.187 , pp. 8172-8180
    • Chromy, B.A.1    Choi, M.W.2    Murphy, G.A.3    Gonzales, A.D.4
  • 151
    • 13844319215 scopus 로고    scopus 로고
    • Analysis of the Listeria cell wall proteome by two-dimensional nanoliquid chromatography coupled to mass spectrometry
    • Calvo, E., Pucciarelli, M. G., Bierne, H., Cossart, P. et al., Analysis of the Listeria cell wall proteome by two-dimensional nanoliquid chromatography coupled to mass spectrometry. Proteomics 2005, 5, 433-443.
    • (2005) Proteomics , vol.5 , pp. 433-443
    • Calvo, E.1    Pucciarelli, M.G.2    Bierne, H.3    Cossart, P.4
  • 152
    • 0019884562 scopus 로고
    • Bacillus anthracis on Gruinard Island
    • Manchee, R. J., Bacillus anthracis on Gruinard Island. Nature 1981, 294, 254-255.
    • (1981) Nature , vol.294 , pp. 254-255
    • Manchee, R.J.1
  • 153
    • 1242318694 scopus 로고    scopus 로고
    • Identification of proteins in the exosporium of Bacillus anthracis
    • Redmond, C., Baillie, L. W., Hibbs, S., Moir, A. J. et al., Identification of proteins in the exosporium of Bacillus anthracis. Microbiology, 2004, 150, 355-363.
    • (2004) Microbiology , vol.150 , pp. 355-363
    • Redmond, C.1    Baillie, L.W.2    Hibbs, S.3    Moir, A.J.4
  • 154
    • 4444368098 scopus 로고    scopus 로고
    • Identification of Bacillus anthracis proteins associated with germination and early outgrowth by proteomic profiling of anthrax spores
    • Huang, C. M., Foster, K. W., DeSilva, T. S., Van Kampen, K. R. et al., Identification of Bacillus anthracis proteins associated with germination and early outgrowth by proteomic profiling of anthrax spores. Proteomics 2004, 4, 2653-2661.
    • (2004) Proteomics , vol.4 , pp. 2653-2661
    • Huang, C.M.1    Foster, K.W.2    DeSilva, T.S.3    Van Kampen, K.R.4
  • 155
    • 33646558918 scopus 로고    scopus 로고
    • Differential proteomic analysis of the Bacillus anthracis secretome: Distinct plasmid and chromosome CO2-dependent cross talk mechanisms modulate extracellular proteolytic activities
    • Chitlaru, T., Gat, O., Gozlan, Y., Ariel, N. et al., Differential proteomic analysis of the Bacillus anthracis secretome: distinct plasmid and chromosome CO2-dependent cross talk mechanisms modulate extracellular proteolytic activities. J. Bacteriol. 2006, 188, 3551-3571.
    • (2006) J. Bacteriol , vol.188 , pp. 3551-3571
    • Chitlaru, T.1    Gat, O.2    Gozlan, Y.3    Ariel, N.4
  • 156
    • 0034529994 scopus 로고    scopus 로고
    • Latent Mycobacterium tuberculosis-persistence, patience, and winning by waiting
    • Manabe, Y. C., Bishai, W. R., Latent Mycobacterium tuberculosis-persistence, patience, and winning by waiting. Nat. Med. 2000, 6, 1327-1329.
    • (2000) Nat. Med , vol.6 , pp. 1327-1329
    • Manabe, Y.C.1    Bishai, W.R.2
  • 157
    • 9144263752 scopus 로고    scopus 로고
    • Comparative proteome analysis of Mycobacterium tuberculosis grown under aerobic and anaerobic conditions
    • Starck, J., Källenius, G., Marklund, B. I., Andersson, D. I., Akerlund, T.Comparative proteome analysis of Mycobacterium tuberculosis grown under aerobic and anaerobic conditions. Microbiology 2004, 150, 3821-3829.
    • (2004) Microbiology , vol.150 , pp. 3821-3829
    • Starck, J.1    Källenius, G.2    Marklund, B.I.3    Andersson, D.I.4    Akerlund, T.5
  • 158
    • 22144496081 scopus 로고    scopus 로고
    • Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics
    • Sinha, S., Kosalai, K., Arora, S., Namane, A. et al., Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics. Microbiology 2005, 151, 2411-2419.
    • (2005) Microbiology , vol.151 , pp. 2411-2419
    • Sinha, S.1    Kosalai, K.2    Arora, S.3    Namane, A.4
  • 159
    • 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
  • 160
    • 84909893350 scopus 로고
    • Virus of avian myeloblastosis (Bai strain A). XXV. Ultracytochemical study of virus and myeloblast phosphatase activity
    • Theg, D. E., Becker, C., Beard, J. W., Virus of avian myeloblastosis (Bai strain A). XXV. Ultracytochemical study of virus and myeloblast phosphatase activity J. Natl. Cancer Inst. 1964, 32, 201-235.
    • (1964) J. Natl. Cancer Inst , vol.32 , pp. 201-235
    • Theg, D.E.1    Becker, C.2    Beard, J.W.3
  • 161
    • 0014755412 scopus 로고
    • G (Gross) and H-2 cell-surface antigens: Location on Gross leukemia cells by electron microscopy with visually labeled antibody
    • Aoki, T., Boyse, E. A., Old, L. J., De Harven, E. et al., G (Gross) and H-2 cell-surface antigens: location on Gross leukemia cells by electron microscopy with visually labeled antibody. Proc. Natl. Acad. Sci. USA 1970, 65, 569-576.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.65 , pp. 569-576
    • Aoki, T.1    Boyse, E.A.2    Old, L.J.3    De Harven, E.4
  • 162
    • 0017581358 scopus 로고
    • Selective incorporation of H-2 antigenic determinants into Friend virus particles
    • Bubbers, J. E., Lilly, F., Selective incorporation of H-2 antigenic determinants into Friend virus particles. Nature 1977, 266, 458-459.
    • (1977) Nature , vol.266 , pp. 458-459
    • Bubbers, J.E.1    Lilly, F.2
  • 163
    • 0018648393 scopus 로고
    • Incorporation of HLA antigens into the envelope of RNA tumor viruses grown in human cells
    • Azocar, J., Essex, M., Incorporation of HLA antigens into the envelope of RNA tumor viruses grown in human cells. Cancer Res. 1979, 39, 3388-3391.
    • (1979) Cancer Res , vol.39 , pp. 3388-3391
    • Azocar, J.1    Essex, M.2
  • 164
    • 0017741124 scopus 로고
    • Histones: Metabolism in simian virus 40-infected cells and incorporation into virions
    • Tan, K.B., Histones: metabolism in simian virus 40-infected cells and incorporation into virions. Proc. Natl. Acad. Sci. USA 1977, 74, 2805-2809.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2805-2809
    • Tan, K.B.1
  • 165
    • 0020966332 scopus 로고
    • Specific selection of host cell glycoproteins during assembly of murine leukaemia virus and vesicular stomatitis virus: Presence of Thy-1 glycoprotein and absence of H-2, Pgp-1 and T-200 glycoproteins on the envelopes of these virus particles
    • Calafat, J., Janssen, H., Démant, P., Hilgers, J., Závada, J., Specific selection of host cell glycoproteins during assembly of murine leukaemia virus and vesicular stomatitis virus: presence of Thy-1 glycoprotein and absence of H-2, Pgp-1 and T-200 glycoproteins on the envelopes of these virus particles. J. Gen. Virol. 1983, 64, 1241-1253.
    • (1983) J. Gen. Virol , vol.64 , pp. 1241-1253
    • Calafat, J.1    Janssen, H.2    Démant, P.3    Hilgers, J.4    Závada, J.5
  • 166
    • 0020556228 scopus 로고
    • Association of human T-cell leukaemia/lymphoma virus with the Tac antigen marker for the human T-cell growth factor receptor
    • Lando, Z., Sarin, P., Megson, M., Greene, W.C. et al., Association of human T-cell leukaemia/lymphoma virus with the Tac antigen marker for the human T-cell growth factor receptor. Nature 1983, 305, 733-736.
    • (1983) Nature , vol.305 , pp. 733-736
    • Lando, Z.1    Sarin, P.2    Megson, M.3    Greene, W.C.4
  • 167
    • 0028862038 scopus 로고
    • Host cell-derived complement control proteins CD55 and CD59 are incorporated into the virions of two unrelated enveloped viruses. Human T cell leukemia/lymphoma virus type I (HTLV-I) and human cytomegalovirus (HCMV)
    • Spear, G. T., Lurain, N. S., Parker, C. J., Ghassemi, M. et al., Host cell-derived complement control proteins CD55 and CD59 are incorporated into the virions of two unrelated enveloped viruses. Human T cell leukemia/lymphoma virus type I (HTLV-I) and human cytomegalovirus (HCMV). J. Immunol. 1995, 155, 4376-4381.
    • (1995) J. Immunol , vol.155 , pp. 4376-4381
    • Spear, G.T.1    Lurain, N.S.2    Parker, C.J.3    Ghassemi, M.4
  • 168
    • 0025702622 scopus 로고
    • Efficient incorporation of human CD4 protein into avian leukosis virus particles
    • Young, J. A., Bates, P., Willert, K., Varmus, H. E., Efficient incorporation of human CD4 protein into avian leukosis virus particles. Science 1990, 250, 1421-1423.
    • (1990) Science , vol.250 , pp. 1421-1423
    • Young, J.A.1    Bates, P.2    Willert, K.3    Varmus, H.E.4
  • 169
    • 0028820613 scopus 로고
    • Epstein-Barr virus infection of CR2-transfected epithelial cells reveals the presence of MHC class II on the virion
    • Knox, P. G., Young, L. S., Epstein-Barr virus infection of CR2-transfected epithelial cells reveals the presence of MHC class II on the virion. Virology 1995, 213, 147-157.
    • (1995) Virology , vol.213 , pp. 147-157
    • Knox, P.G.1    Young, L.S.2
  • 170
    • 0029043553 scopus 로고
    • Host cellular annexin II is associated with cytomegalovirus particles isolated from cultured human fibroblasts
    • Wright, J. F., Kurosky, A., Pryzdial, E. L., Wasi, S., Host cellular annexin II is associated with cytomegalovirus particles isolated from cultured human fibroblasts. J. Virol. 1995, 69, 4784-4791.
    • (1995) J. Virol , vol.69 , pp. 4784-4791
    • Wright, J.F.1    Kurosky, A.2    Pryzdial, E.L.3    Wasi, S.4
  • 171
    • 9044219847 scopus 로고    scopus 로고
    • Human cytomegalovirus carries serine/threonine protein phosphatases PP1 and a host-cell derived PP2A
    • Michelson, S., Turowski, P., Picard, L., Goris, J. et al., Human cytomegalovirus carries serine/threonine protein phosphatases PP1 and a host-cell derived PP2A. J. Virol. 1996, 70, 1415-1423.
    • (1996) J. Virol , vol.70 , pp. 1415-1423
    • Michelson, S.1    Turowski, P.2    Picard, L.3    Goris, J.4
  • 172
    • 0023112323 scopus 로고
    • Direct identification of class II histocompatibility DR proteins in preparations of human T-cell lymphotropic virus type III
    • Henderson, L. E., Sowder, R., Copeland, T. D., Oroszlan, S. et al., Direct identification of class II histocompatibility DR proteins in preparations of human T-cell lymphotropic virus type III. J. Virol. 1987, 61, 629-632.
    • (1987) J. Virol , vol.61 , pp. 629-632
    • Henderson, L.E.1    Sowder, R.2    Copeland, T.D.3    Oroszlan, S.4
  • 173
    • 0033771053 scopus 로고    scopus 로고
    • correlation with stage of disease and presence of opportunistic infection
    • Incorporation of HLA-DR into the envelope of human immunodeficiency virus type 1 in vivo
    • Lawn, S. D., Butera, S. T., Incorporation of HLA-DR into the envelope of human immunodeficiency virus type 1 in vivo: correlation with stage of disease and presence of opportunistic infection. J. Virol. 2000, 74, 10256-10259.
    • (2000) J. Virol , vol.74 , pp. 10256-10259
    • Lawn, S.D.1    Butera, S.T.2
  • 174
    • 0029836852 scopus 로고    scopus 로고
    • Cytoskeletal proteins inside human immunodeficiency virus type 1 virions
    • Ott, D. E., Coren, L. V., Kane, B. P., Busch, L. K. et al., Cytoskeletal proteins inside human immunodeficiency virus type 1 virions. J. Virol. 1996, 70, 7734-7343.
    • (1996) J. Virol , vol.70 , pp. 7734-7343
    • Ott, D.E.1    Coren, L.V.2    Kane, B.P.3    Busch, L.K.4
  • 175
    • 0032975591 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 derived from cocultures of immature dendritic cells with autologous T cells carries T-cell-specific molecules on its surface and is highly infectious
    • Frank, I., Kacani, L., Stoiber, H., Stossel, H. et al., Human immunodeficiency virus type 1 derived from cocultures of immature dendritic cells with autologous T cells carries T-cell-specific molecules on its surface and is highly infectious. J. Virol. 1999, 73, 3449-3454.
    • (1999) J. Virol , vol.73 , pp. 3449-3454
    • Frank, I.1    Kacani, L.2    Stoiber, H.3    Stossel, H.4
  • 176
    • 0034973233 scopus 로고    scopus 로고
    • Differential incorporation of CD45, CD80 (B7-1), CD86 (B7-2), and major histocompatibility complex class I and II molecules into human immunodeficiency virus type 1 virions and microvesicles: Implications for viral pathogenesis and immune regulation
    • Esser, M. T., Graham, D. R., Coren, L. V., Trubey, C. M. et al., Differential incorporation of CD45, CD80 (B7-1), CD86 (B7-2), and major histocompatibility complex class I and II molecules into human immunodeficiency virus type 1 virions and microvesicles: implications for viral pathogenesis and immune regulation. J. Virol. 2001, 75, 6173-6182.
    • (2001) J. Virol , vol.75 , pp. 6173-6182
    • Esser, M.T.1    Graham, D.R.2    Coren, L.V.3    Trubey, C.M.4
  • 177
    • 0035794198 scopus 로고    scopus 로고
    • Attachment of human immunodeficiency virus-1 (HIV-1) particles bearing host-encoded B7-2 proteins leads to nuclear factor-kappa B- and nuclear factor of activated T cells-dependent activation of HIV-1 long terminal repeat transcription
    • Bounou, S., Dumais, N., Tremblay, M. J., Attachment of human immunodeficiency virus-1 (HIV-1) particles bearing host-encoded B7-2 proteins leads to nuclear factor-kappa B- and nuclear factor of activated T cells-dependent activation of HIV-1 long terminal repeat transcription. J. Biol. Chem. 2001, 276, 6359-6369.
    • (2001) J. Biol. Chem , vol.276 , pp. 6359-6369
    • Bounou, S.1    Dumais, N.2    Tremblay, M.J.3
  • 179
    • 0033047267 scopus 로고    scopus 로고
    • Host protein incorporation is conserved among diverse HIV-1 subtypes
    • Roberts, B. D., Butera, S. T., Host protein incorporation is conserved among diverse HIV-1 subtypes. AIDS 1999, 13, 425-427.
    • (1999) AIDS , vol.13 , pp. 425-427
    • Roberts, B.D.1    Butera, S.T.2
  • 180
    • 0033989735 scopus 로고    scopus 로고
    • Cellular compartments of human immunodeficiency virus type 1 replication in vivo: Determination by presence of virion-associated host proteins and impact of opportunistic infection
    • Lawn, S. D., Roberts, B. D., Griffin, G. E., Folks, T. M., Butera, S. T., Cellular compartments of human immunodeficiency virus type 1 replication in vivo: determination by presence of virion-associated host proteins and impact of opportunistic infection. J. Virol. 2000, 74, 139-145.
    • (2000) J. Virol , vol.74 , pp. 139-145
    • Lawn, S.D.1    Roberts, B.D.2    Griffin, G.E.3    Folks, T.M.4    Butera, S.T.5
  • 181
    • 0036776606 scopus 로고    scopus 로고
    • Three isoforms of cyclophilin A associated with human immunodeficiency virus type 1 were found by proteomics by using two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time of flight mass spectrometry
    • Misumi, S., Fuchigami, T., Takamune, N., Takahashi, I. et al., Three isoforms of cyclophilin A associated with human immunodeficiency virus type 1 were found by proteomics by using two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time of flight mass spectrometry. J. Virol. 2002, 76, 10000-10008.
    • (2002) J. Virol , vol.76 , pp. 10000-10008
    • Misumi, S.1    Fuchigami, T.2    Takamune, N.3    Takahashi, I.4
  • 182
    • 0028981307 scopus 로고
    • HIV acquires functional adhesion receptors from host cells
    • Guo, M. M., Hildreth, J. E., HIV acquires functional adhesion receptors from host cells. AIDS Res. Hum. Retrovir. 1995, 11, 1007-1013.
    • (1995) AIDS Res. Hum. Retrovir , vol.11 , pp. 1007-1013
    • Guo, M.M.1    Hildreth, J.E.2
  • 183
    • 0029162867 scopus 로고
    • Role of virion-associated glycosylphosphatidylinositol-linked proteins CD55 and CD59 in complement resistance of cell line-derived and primary isolates of HIV-1
    • Saifuddin, M., Parker, C. J., Peeples, M. E. et al., Role of virion-associated glycosylphosphatidylinositol-linked proteins CD55 and CD59 in complement resistance of cell line-derived and primary isolates of HIV-1. J. Exp. Med. 1995, 182, 501-509.
    • (1995) J. Exp. Med , vol.182 , pp. 501-509
    • Saifuddin, M.1    Parker, C.J.2    Peeples, M.E.3
  • 184
    • 0030813504 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 incorporates both glycosyl phosphatidylinositol-anchored CD55 and CD59 and integral membrane CD46 at levels that protect from complement-mediated destruction
    • Saifuddin, M., Hedayati, T., Atkinson, J. P., Holguin, M. H. et al., Human immunodeficiency virus type 1 incorporates both glycosyl phosphatidylinositol-anchored CD55 and CD59 and integral membrane CD46 at levels that protect from complement-mediated destruction. J. Gen. Virol. 1997, 78, 1907-1911.
    • (1997) J. Gen. Virol , vol.78 , pp. 1907-1911
    • Saifuddin, M.1    Hedayati, T.2    Atkinson, J.P.3    Holguin, M.H.4
  • 185
    • 0030945243 scopus 로고    scopus 로고
    • Host cell-dependent alterations in envelope components of human immunodeficiency virus type 1 virions
    • Bastiani, L., Laal, S., Kim, M., Zolla-Pazner, S., Host cell-dependent alterations in envelope components of human immunodeficiency virus type 1 virions. J. Virol. 1997, 71, 3444-3450.
    • (1997) J. Virol , vol.71 , pp. 3444-3450
    • Bastiani, L.1    Laal, S.2    Kim, M.3    Zolla-Pazner, S.4
  • 186
    • 0024385412 scopus 로고
    • Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation
    • Hildreth, J. E., Orentas, R. J., Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation. Science 1989, 244, 1075-1078.
    • (1989) Science , vol.244 , pp. 1075-1078
    • Hildreth, J.E.1    Orentas, R.J.2
  • 187
    • 0036147255 scopus 로고    scopus 로고
    • Presence of host ICAM-1 in laboratory and clinical strains of human immunodeficiency virus type 1 increases virus infectivity and CD4(+)-T-cell depletion in human lymphoid tissue, a major site of replication in vivo
    • Bounou, S., Leclerc, J. E., Tremblay, M. J., Presence of host ICAM-1 in laboratory and clinical strains of human immunodeficiency virus type 1 increases virus infectivity and CD4(+)-T-cell depletion in human lymphoid tissue, a major site of replication in vivo. J. Virol. 2002, 76, 1004-14.
    • (2002) J. Virol , vol.76 , pp. 1004-1014
    • Bounou, S.1    Leclerc, J.E.2    Tremblay, M.J.3
  • 188
    • 0030962180 scopus 로고    scopus 로고
    • Contribution of virion ICAM-1 to human immunodeficiency virus infectivity and sensitivity to neutralization
    • Rizzuto, C. D., Sodroski, J. G., Contribution of virion ICAM-1 to human immunodeficiency virus infectivity and sensitivity to neutralization. J. Virol. 1997, 71, 4847-4851.
    • (1997) J. Virol , vol.71 , pp. 4847-4851
    • Rizzuto, C.D.1    Sodroski, J.G.2
  • 189
    • 0028979183 scopus 로고
    • HIV type 1 grown on interferon gamma-treated U937 cells shows selective increase in virion-associated intercellular adhesion molecule 1 and HLA-DR and enhanced infectivity for CD4-negative cells
    • Castilletti, C., Capobianchi, M. R., Fais, S. Gentile M. et al., HIV type 1 grown on interferon gamma-treated U937 cells shows selective increase in virion-associated intercellular adhesion molecule 1 and HLA-DR and enhanced infectivity for CD4-negative cells. AIDS Res. Hum. Retrovir. 1995, 11, 547-553.
    • (1995) AIDS Res. Hum. Retrovir , vol.11 , pp. 547-553
    • Castilletti, C.1    Capobianchi, M.R.2    Fais, S.3    Gentile, M.4
  • 190
    • 0030844666 scopus 로고    scopus 로고
    • The acquisition of host-derived major histocompatibility complex class II glycoproteins by human immunodeficiency virus type 1 accelerates the process of virus entry and infection in human T-lymphoid cells
    • Cantin, R., Fortin, J.F., Lamontagne, G., Tremblay, M., The acquisition of host-derived major histocompatibility complex class II glycoproteins by human immunodeficiency virus type 1 accelerates the process of virus entry and infection in human T-lymphoid cells. Blood 1997, 90, 1091-1100.
    • (1997) Blood , vol.90 , pp. 1091-1100
    • Cantin, R.1    Fortin, J.F.2    Lamontagne, G.3    Tremblay, M.4
  • 191
    • 0031054644 scopus 로고    scopus 로고
    • The presence of host-derived HLA-DRI on human immunodeficiency virus type 1 increases viral infectivity
    • Cantin, R., Fortin, J. F., Lamontagne, G., Tremblay, M., The presence of host-derived HLA-DRI on human immunodeficiency virus type 1 increases viral infectivity. J. Virol. 1997, 71, 1922-1930.
    • (1997) J. Virol , vol.71 , pp. 1922-1930
    • Cantin, R.1    Fortin, J.F.2    Lamontagne, G.3    Tremblay, M.4
  • 192
    • 0030894767 scopus 로고    scopus 로고
    • Host-derived ICAM-1 glycoproteins incorporated on human immunodeficiency virus type 1 are biologically active and enhance viral infectivity
    • Fortin, J. F., Cantin, R., Lamontagne, G., Tremblay, M., Host-derived ICAM-1 glycoproteins incorporated on human immunodeficiency virus type 1 are biologically active and enhance viral infectivity. J. Virol. 1997, 71, 3588-3596.
    • (1997) J. Virol , vol.71 , pp. 3588-3596
    • Fortin, J.F.1    Cantin, R.2    Lamontagne, G.3    Tremblay, M.4
  • 193
    • 0035196852 scopus 로고    scopus 로고
    • A novel virus capture assay reveals a differential acquisition of host HLA-DR by clinical isolates of human immunodeficiency virus type 1 expanded in primary human cells depending on the nature of producing cells and the donor source
    • Cantin, R., Martin, G., Tremblay, M. J., A novel virus capture assay reveals a differential acquisition of host HLA-DR by clinical isolates of human immunodeficiency virus type 1 expanded in primary human cells depending on the nature of producing cells and the donor source. J. Gen. Virol. 2001, 82, 2979-2987.
    • (2001) J. Gen. Virol , vol.82 , pp. 2979-2987
    • Cantin, R.1    Martin, G.2    Tremblay, M.J.3
  • 194
    • 0029033175 scopus 로고
    • Progress with gene-product mapping of the Mollicutes: Mycoplasma genitalium
    • Wasinger, V. C., Cordwell, S. J., Cerpa-Poljak, A., Yan, J. X. et al., Progress with gene-product mapping of the Mollicutes: Mycoplasma genitalium. Electrophoresis 1995, 16, 1090-1094.
    • (1995) Electrophoresis , vol.16 , pp. 1090-1094
    • Wasinger, V.C.1    Cordwell, S.J.2    Cerpa-Poljak, A.3    Yan, J.X.4
  • 195
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson, L., Seilhamer, J., A comparison of selected mRNA and protein abundances in human liver. Electrophoresis 1997, 18, 533-537.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 196
    • 0018842660 scopus 로고
    • Shut-off of host protein synthesis in vaccinia-virus-infected cells exposed to cordycepin. A study in vitro
    • Person, A., Beaud, G., Shut-off of host protein synthesis in vaccinia-virus-infected cells exposed to cordycepin. A study in vitro. Eur. J. Biochem. 1980, 103, 85-93.
    • (1980) Eur. J. Biochem , vol.103 , pp. 85-93
    • Person, A.1    Beaud, G.2
  • 197
    • 33947219266 scopus 로고    scopus 로고
    • Large-scale mapping of human protein-protein interactions by mass spectrometry
    • Ewing, R. M., Chu, P., Elisma, F., Li, H. et al., Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol. Syst. Biol. 2007, 3, 89.
    • (2007) Mol. Syst. Biol , vol.3 , pp. 89
    • Ewing, R.M.1    Chu, P.2    Elisma, F.3    Li, H.4
  • 198
    • 0037434980 scopus 로고    scopus 로고
    • From genomics to proteomics
    • Tyers, M., Mann, M., From genomics to proteomics. Nature 2003, 13, 422, 193-197.
    • (2003) Nature , vol.13 , Issue.422 , pp. 193-197
    • Tyers, M.1    Mann, M.2
  • 199
    • 33947408802 scopus 로고    scopus 로고
    • Proteomic analysis and identification of Streptococcus pyogenes surface-associated proteins
    • Severin, A., Nickbarg, E., Wooters, J., Quazi, S. A. et al., Proteomic analysis and identification of Streptococcus pyogenes surface-associated proteins. J. Bacteriol. 2007, 189, 1514-1522.
    • (2007) J. Bacteriol , vol.189 , pp. 1514-1522
    • Severin, A.1    Nickbarg, E.2    Wooters, J.3    Quazi, S.A.4
  • 200
    • 17444403973 scopus 로고    scopus 로고
    • Proteome analysis of membrane and cell wall associated proteins from Staphylococcus aureus
    • Nandakumar, R., Nandakumar, M. P., Marten, M. R., Ross, J. M., Proteome analysis of membrane and cell wall associated proteins from Staphylococcus aureus. J. Proteome Res. 2005, 4, 250-257.
    • (2005) J. Proteome Res , vol.4 , pp. 250-257
    • Nandakumar, R.1    Nandakumar, M.P.2    Marten, M.R.3    Ross, J.M.4
  • 201
    • 25444445823 scopus 로고    scopus 로고
    • Identification of immunogenic and serum binding proteins of Staphylococcus epidermidis
    • Sellman, B. R., Howell, A. P., Kelly-Boyd, C., Baker, S. M., Identification of immunogenic and serum binding proteins of Staphylococcus epidermidis. Infect. Immun. 2005, 73, 6591-6600.
    • (2005) Infect. Immun , vol.73 , pp. 6591-6600
    • Sellman, B.R.1    Howell, A.P.2    Kelly-Boyd, C.3    Baker, S.M.4
  • 202
    • 17644397901 scopus 로고    scopus 로고
    • Surface analyses and immune reactivities of major cell wall-associated proteins of group a streptococcus
    • Cole, J. N., Ramirez, R. D., Currie, B. J., Cordwell, S. J. et al., Surface analyses and immune reactivities of major cell wall-associated proteins of group a streptococcus. Infect. Immun. 2005, 73, 3137-3146.
    • (2005) Infect. Immun , vol.73 , pp. 3137-3146
    • Cole, J.N.1    Ramirez, R.D.2    Currie, B.J.3    Cordwell, S.J.4
  • 203
    • 0036176205 scopus 로고    scopus 로고
    • Identification of major outer surface proteins of Streptococcus agalactiae
    • Hughes, M. J., Moore, J. C., Lane, J. D., Wilson, R. et al., Identification of major outer surface proteins of Streptococcus agalactiae. Infect. Immun. 2002, 70, 1254-1259.
    • (2002) Infect. Immun , vol.70 , pp. 1254-1259
    • Hughes, M.J.1    Moore, J.C.2    Lane, J.D.3    Wilson, R.4
  • 204
    • 8144221393 scopus 로고    scopus 로고
    • Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse
    • Ling, E., Feldman, G., Portnoi, M., Dagan, R. et al., Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse. Clin. Exp. Immunol. 2004, 138, 290-298.
    • (2004) Clin. Exp. Immunol , vol.138 , pp. 290-298
    • Ling, E.1    Feldman, G.2    Portnoi, M.3    Dagan, R.4
  • 205
    • 20644450358 scopus 로고    scopus 로고
    • Proteomic analysis of cell surface proteins from Clostridium difficile
    • Wright, A., Wait, R., Begum, S., Crossett, B. et al., Proteomic analysis of cell surface proteins from Clostridium difficile. Proteomics 2005, 5, 2443-2452.
    • (2005) Proteomics , vol.5 , pp. 2443-2452
    • Wright, A.1    Wait, R.2    Begum, S.3    Crossett, B.4


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