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Volumn 2, Issue 8, 2001, Pages 569-577

Mycobacterium tuberculosis: Here today, and here tomorrow

Author keywords

[No Author keywords available]

Indexed keywords

MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 0035432383     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35085034     Document Type: Review
Times cited : (631)

References (70)
  • 1
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S. T. et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544 (1998).
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1
  • 2
    • 0030331770 scopus 로고    scopus 로고
    • Selective receptor blockade during phagocytosis does not alter the survival and growth of Mycobacterium tuberculosis in human macrophages
    • Zimmerli, S., Edwards, S. & Ernst, J. D. Selective receptor blockade during phagocytosis does not alter the survival and growth of Mycobacterium tuberculosis in human macrophages. Am. J. Respir. Cell. Mol. Biol. 15, 760-770 (1996).
    • (1996) Am. J. Respir. Cell. Mol. Biol. , vol.15 , pp. 760-770
    • Zimmerli, S.1    Edwards, S.2    Ernst, J.D.3
  • 3
    • 0014675606 scopus 로고
    • Mycobacteria and lysosomes: A paradox
    • Brown, C. A., Draper, P. & Hart, P. D. Mycobacteria and lysosomes: a paradox. Nature 221, 658-660 (1969). This is a classic paper that reported the initial observations that Mycobacterium-containing vacuoles failed to fuse with lysosomes.
    • (1969) Nature , vol.221 , pp. 658-660
    • Brown, C.A.1    Draper, P.2    Hart, P.D.3
  • 4
    • 0015334243 scopus 로고
    • Ultrastructural study of the behavior of macrophages toward parasitic mycobacteria
    • Hart, P. D., Armstrong, J. A., Brown, C. A. & Draper, P. Ultrastructural study of the behavior of macrophages toward parasitic mycobacteria. Infect. Immun. 5, 803-807 (1972).
    • (1972) Infect. Immun. , vol.5 , pp. 803-807
    • Hart, P.D.1    Armstrong, J.A.2    Brown, C.A.3    Draper, P.4
  • 5
    • 0016304515 scopus 로고
    • Strain virulence and the lysosomal response in macrophages infected with Mycobacterium tuberculosis
    • Hart, P. D. & Armstrong, J. A. Strain virulence and the lysosomal response in macrophages infected with Mycobacterium tuberculosis. Infect. Immun. 10, 742-746 (1974).
    • (1974) Infect. Immun. , vol.10 , pp. 742-746
    • Hart, P.D.1    Armstrong, J.A.2
  • 6
    • 0016742008 scopus 로고
    • Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual nonfusion pattern and observations on bacterial survival
    • Armstrong, J. A. & Hart, P. D. Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual nonfusion pattern and observations on bacterial survival. J. Exp. Med. 142, 1-16 (1975).
    • (1975) J. Exp. Med. , vol.142 , pp. 1-16
    • Armstrong, J.A.1    Hart, P.D.2
  • 7
    • 0025845247 scopus 로고
    • Evidence that vesicles containing living, virulent Mycobacterium tuberculosis or Mycobacterium avium in cultured human macrophages are not acidic
    • Crowle, A. J., Dahl, R., Ross, E. & May, M. H. Evidence that vesicles containing living, virulent Mycobacterium tuberculosis or Mycobacterium avium in cultured human macrophages are not acidic. Infect. Immun. 59, 1823-1831 (1991).
    • (1991) Infect. Immun. , vol.59 , pp. 1823-1831
    • Crowle, A.J.1    Dahl, R.2    Ross, E.3    May, M.H.4
  • 8
    • 0028220231 scopus 로고
    • Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase
    • Sturgill-Koszycki, S. et al. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science 263, 678-681 (1994). This paper marked the transition from descriptive to experimental, biochemical analysis of the Mycobacterium-containing vacuole and provided an initial explanation as to why these vacuoles failed to acidify.
    • (1994) Science , vol.263 , pp. 678-681
    • Sturgill-Koszycki, S.1
  • 9
    • 0022641016 scopus 로고
    • Evidence for inhibition of fusion of lysosomal and prelysosomal compartments with phagosomes in macrophages infected with pathogenic Mycobacterium avium
    • Frehel, C., de Chastellier, C., Lang, T. & Rastogi, N. Evidence for inhibition of fusion of lysosomal and prelysosomal compartments with phagosomes in macrophages infected with pathogenic Mycobacterium avium. Infect. Immun. 52, 252-262 (1986).
    • (1986) Infect. Immun. , vol.52 , pp. 252-262
    • Frehel, C.1    De Chastellier, C.2    Lang, T.3    Rastogi, N.4
  • 10
    • 0028909199 scopus 로고
    • Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited
    • Clemens, D. L. & Horwitz, M. A. Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited. J. Exp. Med. 181, 257-270 (1995).
    • (1995) J. Exp. Med. , vol.181 , pp. 257-270
    • Clemens, D.L.1    Horwitz, M.A.2
  • 11
    • 0029905151 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered fransferrin
    • Clemens, D. L. & Horwitz, M. A. The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered fransferrin. J. Exp. Med. 184, 1349-1355 (1996). This paper, together with reference 13, showed that the Mycobacterium-containing vacuole was arrested within the transferrin recycling pathway of the host macrophage.
    • (1996) J. Exp. Med. , vol.184 , pp. 1349-1355
    • Clemens, D.L.1    Horwitz, M.A.2
  • 12
    • 0030012842 scopus 로고    scopus 로고
    • Mycobacterium avium- and Mycobacterium tuberculosis-containing vacuoles are dynamic, fusion-competent vesicles that are accessible to glycosphingolipids from the host cell plasmalemma
    • Russell, D. G., Dant, J. & Sturgill-Koszycki, S. Mycobacterium avium-and Mycobacterium tuberculosis-containing vacuoles are dynamic, fusion-competent vesicles that are accessible to glycosphingolipids from the host cell plasmalemma. J. Immunol. 156, 4764-4773 (1996).
    • (1996) J. Immunol. , vol.156 , pp. 4764-4773
    • Russell, D.G.1    Dant, J.2    Sturgill-Koszycki, S.3
  • 13
    • 0030481130 scopus 로고    scopus 로고
    • Mycobacterium-containing phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis
    • Sturgill-Koszycki, S., Schaible, U. E. & Russell, D. G. Mycobacterium-containing phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis. EMBO J. 15, 6960-6968 (1996). This paper provided a fuller understanding that the Mycobacterium-containing vacuole showed limited acidification because it was arrested within the eariy endosomal network and remained accessible to transferrin.
    • (1996) EMBO J. , vol.15 , pp. 6960-6968
    • Sturgill-Koszycki, S.1    Schaible, U.E.2    Russell, D.G.3
  • 14
    • 0032751602 scopus 로고    scopus 로고
    • Direct delivery of procathepsin D to phagosomes: Implications for phagosome biogenesis and parasitism by Mycobacterium
    • Ullrich, H. J., Beatty, W. L. & Russell, D. G. Direct delivery of procathepsin D to phagosomes: implications for phagosome biogenesis and parasitism by Mycobacterium. Eur. J. Cell Biol. 78, 739-748 (1999).
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 739-748
    • Ullrich, H.J.1    Beatty, W.L.2    Russell, D.G.3
  • 15
    • 0029670902 scopus 로고    scopus 로고
    • The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane
    • Rohrer, J., Schweizer, A., Russell, D. & Kornfeld, S. The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J. Cell Biol. 132, 565-576 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 565-576
    • Rohrer, J.1    Schweizer, A.2    Russell, D.3    Kornfeld, S.4
  • 16
    • 0030960157 scopus 로고    scopus 로고
    • Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by rab5 and rab7
    • Via, L. E. et al. Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by rab5 and rab7. J. Biol. Chem. 272, 13326-13331 (1997). This was the first demonstration of the stable association of the early endosomal GTPase Rab5 with the Mycobacterium-containing vacuole.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13326-13331
    • Via, L.E.1
  • 17
    • 0034064659 scopus 로고    scopus 로고
    • Deviant expression of Rab5 on phagosomes containing the intracellufar pathogens Mycobacterium tuberculosis and Legionella pneumophila is associated with altered phagosomal fate
    • Clemens, D. L., Lee, B. Y. & Horwitz, M. A. Deviant expression of Rab5 on phagosomes containing the intracellufar pathogens Mycobacterium tuberculosis and Legionella pneumophila is associated with altered phagosomal fate. Infect. Immun. 68, 2671-2684 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 2671-2684
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 18
    • 0030944210 scopus 로고    scopus 로고
    • Calmodulin regulates endosome fusion
    • Colombo, M. I., Beron, W. & Stahl, P. D. Calmodulin regulates endosome fusion. J. Biol. Chem. 272, 7707-7712 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 7707-7712
    • Colombo, M.I.1    Beron, W.2    Stahl, P.D.3
  • 19
    • 0034677007 scopus 로고    scopus 로고
    • 2+ signaling by Mycobacterium tuberculosis is associated with reduced phagosome-lysosome fusion and increased survival within human macrophages
    • 2+ signaling by Mycobacterium tuberculosis is associated with reduced phagosome-lysosome fusion and increased survival within human macrophages. J. Exp. Med. 191, 287-302 (2000). An extremely interesting experimental study linking calmodulin and calcium to the transition of the Mycobacterium-containing vacuole from an early endosomal to a lysosomal environment.
    • (2000) J. Exp. Med. , vol.191 , pp. 287-302
    • Malik, Z.A.1    Denning, G.M.2    Kusner, D.J.3
  • 20
    • 0035284908 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis phagosomes exhibit altered calmodulin-dependent signal transduction: Contribution to inhibition of phagosome-lysosome fusion and intracellular survival in human macrophages
    • Malik, Z. A., Iyer, S. S. &. Kusner, D. J. Mycobacterium tuberculosis phagosomes exhibit altered calmodulin-dependent signal transduction: contribution to inhibition of phagosome-lysosome fusion and intracellular survival in human macrophages. J. Immunol. 166, 3392-3401 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 3392-3401
    • Malik, Z.A.1    Iyer, S.S.2    Kusner, D.J.3
  • 21
    • 0033553440 scopus 로고    scopus 로고
    • A coat protein on phagosomes involved in the intracellular survival of mycobacteria
    • Ferrari, G., Langen, H., Naito, M. & Pieters, J. A coat protein on phagosomes involved in the intracellular survival of mycobacteria. Cell 97, 435-447 (1999). An interesting description of the stable association of the early phagosome coat protein coronin 1 (TACO) with the Mycobacterium-containing vacuoles.
    • (1999) Cell , vol.97 , pp. 435-447
    • Ferrari, G.1    Langen, H.2    Naito, M.3    Pieters, J.4
  • 22
    • 0029583095 scopus 로고
    • Coronin involved in phagocytosis: Dynamics of particle-induced relocalization visualized by a green fluorescent protein tag
    • Maniak, M., Rauchenberger, R., Albrecht, R., Murphy, J. & Gerisch, G. Coronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein tag. Cell 83, 915-924 (1995).
    • (1995) Cell , vol.83 , pp. 915-924
    • Maniak, M.1    Rauchenberger, R.2    Albrecht, R.3    Murphy, J.4    Gerisch, G.5
  • 23
    • 0034595877 scopus 로고    scopus 로고
    • Essential role for cholesterol in entry of mycobacteria into macrophages
    • Gatfield, J. & Pieters, J. Essential role for cholesterol in entry of mycobacteria into macrophages. Science 288, 1647-1650 (2000).
    • (2000) Science , vol.288 , pp. 1647-1650
    • Gatfield, J.1    Pieters, J.2
  • 24
    • 0030273597 scopus 로고    scopus 로고
    • Host signal transduction and endocytosis of Campylobacter jejuni
    • Wooldridge, K. G., Williams, P. H. & Ketley, J. M. Host signal transduction and endocytosis of Campylobacter jejuni. Microb. Pathog. 21, 299-305 (1996).
    • (1996) Microb. Pathog. , vol.21 , pp. 299-305
    • Wooldridge, K.G.1    Williams, P.H.2    Ketley, J.M.3
  • 25
    • 0034326660 scopus 로고    scopus 로고
    • Nonopsonic phagocytosis of Mycobacterium kansasii by human neutrophils depends on cholesterol and is mediated by CR3 associated with glycosylphosphatidylinositol-anchored proteins
    • Peyron, P., Bordier, C., N'Diaye, E. N. & Maridonneau-Parini, I. Nonopsonic phagocytosis of Mycobacterium kansasii by human neutrophils depends on cholesterol and is mediated by CR3 associated with glycosylphosphatidylinositol-anchored proteins. J. Immunol. 165, 5186-5191 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 5186-5191
    • Peyron, P.1    Bordier, C.2    N'Diaye, E.N.3    Maridonneau-Parini, I.4
  • 26
    • 0033962110 scopus 로고    scopus 로고
    • Genetic susceptibility to intracellular infections: Nramp1, macrophage function and divalent cations transport
    • Gruenheid, S. & Gros, P. Genetic susceptibility to intracellular infections: Nramp1, macrophage function and divalent cations transport. Curr. Opin. Microbiol. 3, 43-48 (2000).
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 43-48
    • Gruenheid, S.1    Gros, P.2
  • 28
    • 0031850526 scopus 로고    scopus 로고
    • Host resistance to intracellular infection: Mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification
    • Hackam, D. J. et al. Host resistance to intracellular infection: mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification. J. Exp. Med. 188, 351-364 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 351-364
    • Hackam, D.J.1
  • 29
    • 0035868324 scopus 로고    scopus 로고
    • -/bivalent cation antiporter
    • -/bivalent cation antiporter. Biochem. J. 354, 511-519 (2001).
    • (2001) Biochem. J. , vol.354 , pp. 511-519
    • Goswami, T.1
  • 30
    • 0346695147 scopus 로고    scopus 로고
    • Natural resistance to intracellular infections: Natural resistance associated macrophage protein 1 (NRAMP1) functions as a pH-dependent manganese transporter at the phagosomal membrane
    • Jabado, N. et al. Natural resistance to intracellular infections: natural resistance associated macrophage protein 1 (NRAMP1) functions as a pH-dependent manganese transporter at the phagosomal membrane. J. Exp. Med. 191, 1-12 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1-12
    • Jabado, N.1
  • 31
    • 0019315920 scopus 로고
    • Ammonia inhibits phagosome-lysosome fusion in macrophages
    • Gordon, A. H., Hart, P. D. & Young, M. R. Ammonia inhibits phagosome-lysosome fusion in macrophages. Nature 286, 79-80 (1980).
    • (1980) Nature , vol.286 , pp. 79-80
    • Gordon, A.H.1    Hart, P.D.2    Young, M.R.3
  • 32
    • 0029775018 scopus 로고    scopus 로고
    • Urease activity does not contribute dramatically to persistence of Mycobacterium bovis bacillus Calmette-Guérin
    • Reyrat, J. M., Lopez-Ramirez, G., Ofredo, C., Gicquel, B. & Winter, N. Urease activity does not contribute dramatically to persistence of Mycobacterium bovis bacillus Calmette-Guérin. Infect. Immun. 64, 3934-3936 (1996).
    • (1996) Infect. Immun. , vol.64 , pp. 3934-3936
    • Reyrat, J.M.1    Lopez-Ramirez, G.2    Ofredo, C.3    Gicquel, B.4    Winter, N.5
  • 33
    • 0028793282 scopus 로고
    • Phagocytic processing of the macrophage endoparasite, Mycobacterium avium, in comparison to phagosomes which contain Bacillus subtilis or latex beads
    • de Chastellier, C., Lang, T. & Thilo, L. Phagocytic processing of the macrophage endoparasite, Mycobacterium avium, in comparison to phagosomes which contain Bacillus subtilis or latex beads. Eur. J. Cell Biol. 68, 167-182 (1995).
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 167-182
    • De Chastellier, C.1    Lang, T.2    Thilo, L.3
  • 34
    • 0030024022 scopus 로고    scopus 로고
    • Different fates of phagocytosed particles after delivery into macrophage lysosomes
    • Oh, Y. K. & Swanson, J. A. Different fates of phagocytosed particles after delivery into macrophage lysosomes. J. Cell Biol. 132, 585-593 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 585-593
    • Oh, Y.K.1    Swanson, J.A.2
  • 35
    • 0031914958 scopus 로고    scopus 로고
    • Cytokine activation leads to acidification and increases maturation of Mycobacterium avium-containing phagosomes in murine macrophages
    • Schaible, U. E., Sturgill-Koszycki, S., Schlesinger, P. H. & Russell, D. G. Cytokine activation leads to acidification and increases maturation of Mycobacterium avium-containing phagosomes in murine macrophages. J. Immunol. 160, 1290-1296 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 1290-1296
    • Schaible, U.E.1    Sturgill-Koszycki, S.2    Schlesinger, P.H.3    Russell, D.G.4
  • 36
    • 2642649500 scopus 로고    scopus 로고
    • Effects of cytokines on mycobacterial phagosome maturation
    • Via, L. E. et al. Effects of cytokines on mycobacterial phagosome maturation. J. Cell Sci. 111, 897-905 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 897-905
    • Via, L.E.1
  • 37
    • 0031010661 scopus 로고    scopus 로고
    • Identification of nitric oxide synthase as a protective locus against tuberculosis
    • MacMicking, J. D. et al. Identification of nitric oxide synthase as a protective locus against tuberculosis. Proc. Natl Acad. Sci. USA 94, 5243-5248 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5243-5248
    • MacMicking, J.D.1
  • 38
    • 0029035476 scopus 로고
    • Altered immune responses in mice lacking inducible nitric oxide synthase
    • Wei, X. Q. et al. Altered immune responses in mice lacking inducible nitric oxide synthase. Nature 375, 408-411 (1995).
    • (1995) Nature , vol.375 , pp. 408-411
    • Wei, X.Q.1
  • 39
    • 0028936417 scopus 로고
    • Effects of nitric oxide synthase inhibitors on murine infection with Mycobacterium tuberculosis
    • Chan, J., Tanaka, K., Carroll, D., Flynn, J. & Bloom, B. R. Effects of nitric oxide synthase inhibitors on murine infection with Mycobacterium tuberculosis. Infect. Immun. 63, 736-740 (1995).
    • (1995) Infect. Immun. , vol.63 , pp. 736-740
    • Chan, J.1    Tanaka, K.2    Carroll, D.3    Flynn, J.4    Bloom, B.R.5
  • 40
    • 0029995158 scopus 로고    scopus 로고
    • Characterization of the Mycobacterium tuberculosis phagosome
    • Clemens, D. L. Characterization of the Mycobacterium tuberculosis phagosome. Trends Microbiol. 4, 113-118 (1996).
    • (1996) Trends Microbiol. , vol.4 , pp. 113-118
    • Clemens, D.L.1
  • 41
    • 0034548704 scopus 로고    scopus 로고
    • Interaction of Mycobacterium avium-containing phagosomes with the antigen presentation pathway
    • Ullrich, H. J., Beatty, W. L. & Russell, D. G. Interaction of Mycobacterium avium-containing phagosomes with the antigen presentation pathway. J. Immunol. 165, 6073-6080 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 6073-6080
    • Ullrich, H.J.1    Beatty, W.L.2    Russell, D.G.3
  • 43
    • 0028997805 scopus 로고
    • The inhibitory effects of Mycobacterium tuberculosis on MHC class II expression by monocytes activated with riminophenazines and phagocyte stimulants
    • Wadee, A. A., Kuschke, R. H. & Dooms, T. G. The inhibitory effects of Mycobacterium tuberculosis on MHC class II expression by monocytes activated with riminophenazines and phagocyte stimulants. Clin. Exp. Immunol. 100, 434-439 (1995).
    • (1995) Clin. Exp. Immunol. , vol.100 , pp. 434-439
    • Wadee, A.A.1    Kuschke, R.H.2    Dooms, T.G.3
  • 44
    • 0033197959 scopus 로고    scopus 로고
    • Attenuation of MHC class II expression in macrophages infected with Mycobacterium bovis bacillus Calmette-Guérin involves class II transactivator and depends on the Nramp1 gene
    • Wojciechowski, W., DeSanctis, J., Skamene, E. & Radzioch, D. Attenuation of MHC class II expression in macrophages infected with Mycobacterium bovis bacillus Calmette-Guérin involves class II transactivator and depends on the Nramp1 gene. J. Immunol. 163, 2688-2696 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 2688-2696
    • Wojciechowski, W.1    DeSanctis, J.2    Skamene, E.3    Radzioch, D.4
  • 45
    • 0032194116 scopus 로고    scopus 로고
    • Down-regulation of CD1 on antigen-presenting cells by infection with Mycobacterium tuberculosis
    • Sienger, S., Niazi, K. R. & Modlin, R. L. Down-regulation of CD1 on antigen-presenting cells by infection with Mycobacterium tuberculosis. J. Immunol. 161, 3582-3588 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 3582-3588
    • Sienger, S.1    Niazi, K.R.2    Modlin, R.L.3
  • 46
    • 0034630456 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis inhibits MHC class II antigen processing in murine bone marrow macrophages
    • Noss, E. H., Harding, C. V. & Boom, W. H. Mycobacterium tuberculosis inhibits MHC class II antigen processing in murine bone marrow macrophages. Cell. Immunol. 201, 63-74 (2000).
    • (2000) Cell. Immunol. , vol.201 , pp. 63-74
    • Noss, E.H.1    Harding, C.V.2    Boom, W.H.3
  • 47
    • 0030639114 scopus 로고    scopus 로고
    • IL-6 produced by macrophages infected with Mycobacterium species suppresses T cell responses
    • VanHeyningen, T. K., Collins, H. L. & Russell, D. G. IL-6 produced by macrophages infected with Mycobacterium species suppresses T cell responses. J. Immunol. 158, 330-337 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 330-337
    • VanHeyningen, T.K.1    Collins, H.L.2    Russell, D.G.3
  • 48
    • 0033214553 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis inhibits IFN-γ transcriptional responses without inhibiting activation of STAT1
    • Ting, L. M., Kim, A. C., Cattamanchi, A. & Ernst, J. D. Mycobacterium tuberculosis inhibits IFN-γ transcriptional responses without inhibiting activation of STAT1. J. Immunol. 163, 3898-3906 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 3898-3906
    • Ting, L.M.1    Kim, A.C.2    Cattamanchi, A.3    Ernst, J.D.4
  • 49
    • 0030931885 scopus 로고    scopus 로고
    • Conditionally replicating mycobacteriophages: A system for transposon delivery to Mycobacterium tuberculosis
    • Bardarov, S. et al. Conditionally replicating mycobacteriophages: a system for transposon delivery to Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 94, 10961-10966 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10961-10966
    • Bardarov, S.1
  • 50
    • 0030961089 scopus 로고    scopus 로고
    • Efficient allelic exchange and transposon mutagenesis in Mycobacterium tuberculosis
    • Pelicic, V. et al. Efficient allelic exchange and transposon mutagenesis in Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 94, 10955-10960 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10955-10960
    • Pelicic, V.1
  • 51
    • 0000812428 scopus 로고    scopus 로고
    • Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis
    • Camacho, L. R., Ensergueix, D., Perez, E., Gicquel, B. & Guilhot, C. Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis. Mol. Microbiol. 34, 257-267 (1999).
    • (1999) Mol. Microbiol. , vol.34 , pp. 257-267
    • Camacho, L.R.1    Ensergueix, D.2    Perez, E.3    Gicquel, B.4    Guilhot, C.5
  • 52
    • 0033523971 scopus 로고    scopus 로고
    • Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice
    • Cox, J. S., Chen, B., McNeil, M. & Jacobs, W. R. Jr Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature 402, 79-83 (1999).
    • (1999) Nature , vol.402 , pp. 79-83
    • Cox, J.S.1    Chen, B.2    McNeil, M.3    Jacobs Jr., W.R.4
  • 53
    • 0034157346 scopus 로고    scopus 로고
    • Trafficking and release of mycobacterial lipids from infected macrophages
    • Beatty, W. B., Rhoades, E. R., Ullrich, H. J., Chatterjee, D. & Russell, D. G. Trafficking and release of mycobacterial lipids from infected macrophages. Traffic 1, 235-247 (2000).
    • (2000) Traffic , vol.1 , pp. 235-247
    • Beatty, W.B.1    Rhoades, E.R.2    Ullrich, H.J.3    Chatterjee, D.4    Russell, D.G.5
  • 54
    • 0034443580 scopus 로고    scopus 로고
    • Identification of mycobacterial surface proteins released into subcellular compartments of infected macrophages
    • Beatty, W. L. & Russell, D. G. Identification of mycobacterial surface proteins released into subcellular compartments of infected macrophages. Infect. Immunol. 68, 6997-7002 (2000).
    • (2000) Infect. Immunol. , vol.68 , pp. 6997-7002
    • Beatty, W.L.1    Russell, D.G.2
  • 55
    • 0035132517 scopus 로고    scopus 로고
    • Mycobacterial surface moieties are released from infected macrophages by a constitutive exocytic event
    • Beatty, W. L., Ullrich, H. J. & Russell, D. G. Mycobacterial surface moieties are released from infected macrophages by a constitutive exocytic event. Eur. J. Cell. Biol. 80, 31-40 (2001).
    • (2001) Eur. J. Cell. Biol. , vol.80 , pp. 31-40
    • Beatty, W.L.1    Ullrich, H.J.2    Russell, D.G.3
  • 56
    • 0344286166 scopus 로고    scopus 로고
    • Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis
    • Honer Zu Bentrup, K., Miczak, A., Swenson, D. L. & Russell, D. G. Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis. J. Bacteriol. 181, 7161-7167 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 7161-7167
    • Honer Zu Bentrup, K.1    Miczak, A.2    Swenson, D.L.3    Russell, D.G.4
  • 57
    • 0028603583 scopus 로고
    • Dormancy of Mycobacterium tuberculosis and latency of disease
    • Wayne, L. G. Dormancy of Mycobacterium tuberculosis and latency of disease. Eur. J. Clin. Microbiol. Infect. Dis. 13, 908-914 (1994).
    • (1994) Eur. J. Clin. Microbiol. Infect. Dis. , vol.13 , pp. 908-914
    • Wayne, L.G.1
  • 58
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence
    • Wayne, L. G. & Hayes, L. G. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence. Infect. Immun. 64, 2062-2069 (1996).
    • (1996) Infect. Immun. , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 59
    • 0342794213 scopus 로고    scopus 로고
    • Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase
    • McKinney, J. D. et al. Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 406, 735-738 (2000). This is the first demonstration that the changing intracellular environment of an activated, versus a resting, macrophage culminates in a shift in metabolism in the infecting Mycobacterium.
    • (2000) Nature , vol.406 , pp. 735-738
    • McKinney, J.D.1
  • 60
    • 0033756894 scopus 로고    scopus 로고
    • Rab5 regulates the kiss and run fusion between phagosomes and endosomes and the acquisition of phagosome leishmanicidal properties in RAW 264.7 macrophages
    • Duclos, S. et al. Rab5 regulates the kiss and run fusion between phagosomes and endosomes and the acquisition of phagosome leishmanicidal properties in RAW 264.7 macrophages. J. Cell Sci. 113, 3531-3541 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 3531-3541
    • Duclos, S.1
  • 61
    • 0034685807 scopus 로고    scopus 로고
    • Characterization of rapid membrane internalization and recycling
    • Hao, M. & Maxfield, F. R. Characterization of rapid membrane internalization and recycling. J. Biol. Chem. 275, 15279-15286 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 15279-15286
    • Hao, M.1    Maxfield, F.R.2
  • 62
    • 0029670903 scopus 로고    scopus 로고
    • Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting
    • Schweizer, A., Kornfeld, S. & Rohrer, J. Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. J. Cell Biol. 132, 577-584 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 577-584
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 63
    • 0032234895 scopus 로고    scopus 로고
    • Vaccines, genes and trials
    • Fine, P. E. Vaccines, genes and trials. Novartis Found. Symp. 217, 57-69 (1998).
    • (1998) Novartis Found. Symp. , vol.217 , pp. 57-69
    • Fine, P.E.1
  • 64
    • 0033826580 scopus 로고    scopus 로고
    • Is the development of a new tuberculosis vaccine possible?
    • Kaufmann, S. H. Is the development of a new tuberculosis vaccine possible? Nature Med. 6, 955-960 (2000).
    • (2000) Nature Med. , vol.6 , pp. 955-960
    • Kaufmann, S.H.1
  • 66
    • 0031745342 scopus 로고    scopus 로고
    • Commentary: Making tuberculosis treatment available for all
    • Maher, D. & Nunn, P. Commentary: making tuberculosis treatment available for all. Bull. World Health Organ. 76, 125-126 (1998).
    • (1998) Bull. World Health Organ. , vol.76 , pp. 125-126
    • Maher, D.1    Nunn, P.2
  • 67
    • 0032838896 scopus 로고    scopus 로고
    • Directly observed therapy, short-course: The best way to prevent multidrug-resistant tuberculosis
    • Yew, W. W. Directly observed therapy, short-course: the best way to prevent multidrug-resistant tuberculosis. Chemotherapy 45, 26-33 (1999).
    • (1999) Chemotherapy , vol.45 , pp. 26-33
    • Yew, W.W.1
  • 68
    • 0035182257 scopus 로고    scopus 로고
    • Dormant tubercle bacilli: The key to more effective TB chemotherapy?
    • Dick, T. Dormant tubercle bacilli: the key to more effective TB chemotherapy? J. Antimicrob. Chemother. 47, 117-118 (2001).
    • (2001) J. Antimicrob. Chemother. , vol.47 , pp. 117-118
    • Dick, T.1
  • 69
    • 0034528573 scopus 로고    scopus 로고
    • In vivo veritas: The search for TB drug targets goes live
    • McKinney, J. D. In vivo veritas: the search for TB drug targets goes live. Nature Med. 6, 1330-1333 (2000).
    • (2000) Nature Med. , vol.6 , pp. 1330-1333
    • McKinney, J.D.1
  • 70
    • 0033986977 scopus 로고    scopus 로고
    • Use of genomics and combinatorial chemistry in the development of new antimycobacterial drugs
    • Barry, C. E., Slayden, R. A., Sampson, A. E. & Lee, R. E. Use of genomics and combinatorial chemistry in the development of new antimycobacterial drugs. Biochem. Pharmacol. 59, 221-231 (2000).
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 221-231
    • Barry, C.E.1    Slayden, R.A.2    Sampson, A.E.3    Lee, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.