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Volumn 406, Issue 6797, 2000, Pages 768-774

Pathogenic strategies of enteric bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN FILAMENT; BACTERIAL VIRULENCE; CYTOSKELETON; ENTEROBACTERIACEAE; GRAM NEGATIVE INFECTION; HUMAN; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; REVIEW;

EID: 0034680103     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35021212     Document Type: Review
Times cited : (125)

References (54)
  • 2
    • 0032482924 scopus 로고    scopus 로고
    • Molecular archaeology of the Escherichia coli genome
    • Lawrence, J. G. & Ochman, H. Molecular archaeology of the Escherichia coli genome. Proc. Natl. Acad. Sci. USA 95, 9413-9417 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9413-9417
    • Lawrence, J.G.1    Ochman, H.2
  • 3
    • 0030057090 scopus 로고    scopus 로고
    • Lysogenic conversion by a filamentous phage encoding cholera toxin
    • Waldor, M. K. & Mekalanos, J. J. Lysogenic conversion by a filamentous phage encoding cholera toxin. Science 272, 1910-1914 (1996).
    • (1996) Science , vol.272 , pp. 1910-1914
    • Waldor, M.K.1    Mekalanos, J.J.2
  • 4
    • 0033609358 scopus 로고    scopus 로고
    • A bacteriophage encoding a pathogenicity island, a type-IV pilus and a phage receptor in cholera bacteria
    • Karaolis, D. K., Somara, S., Maneval, D. R. Jr, Johnson, J. A. & Kaper, J. B. A bacteriophage encoding a pathogenicity island, a type-IV pilus and a phage receptor in cholera bacteria. Nature 399, 375-379 (1999)
    • (1999) Nature , vol.399 , pp. 375-379
    • Karaolis, D.K.1    Somara, S.2    Maneval D.R., Jr.3    Johnson, J.A.4    Kaper, J.B.5
  • 5
    • 0031823632 scopus 로고    scopus 로고
    • Molecular evolution of a pathogenicity island from enterohemorrhagic Escherichia coli O157:H7
    • Perna, N. T. et al. Molecular evolution of a pathogenicity island from enterohemorrhagic Escherichia coli O157:H7. Infect. Immun. 66, 3810-3817 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 3810-3817
    • Perna, N.T.1
  • 6
    • 0032035356 scopus 로고    scopus 로고
    • The chaperone/usher pathway: A major terminal branch of the general secretory pathway
    • Thanassi, D. G., Saulino, E. T. & Hultgren, S. J. The chaperone/usher pathway: a major terminal branch of the general secretory pathway. Curr. Opin. Microbiol. 1, 221-231 (1998).
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 221-231
    • Thanassi, D.G.1    Saulino, E.T.2    Hultgren, S.J.3
  • 7
    • 0032963612 scopus 로고    scopus 로고
    • Twelve pil genes are required for biogenesis of the R64 thin pilus
    • Yoshida, T., Kim, S. R. & Komano, T. Twelve pil genes are required for biogenesis of the R64 thin pilus. J. Bacteriol. 181, 2038-2043 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 2038-2043
    • Yoshida, T.1    Kim, S.R.2    Komano, T.3
  • 8
    • 0034005318 scopus 로고    scopus 로고
    • Effects of bfp mutations on biogenesis of functional enteropathogenic Escherichia coli type IV pili
    • Anantha, R. P., Stone, K. D. & Donnenberg, M. S. Effects of bfp mutations on biogenesis of functional enteropathogenic Escherichia coli type IV pili. J. Bacteriol. 182, 2498-2506 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 2498-2506
    • Anantha, R.P.1    Stone, K.D.2    Donnenberg, M.S.3
  • 9
    • 0033536633 scopus 로고    scopus 로고
    • Crystal structure of invasin: A bacterial integrin-binding protein
    • Hamburger, Z. A., Brown, M. S., Isberg, R. R. & Bjorkman, P. I. Crystal structure of invasin: a bacterial integrin-binding protein. Science 286, 291-255 (1999).
    • (1999) Science , vol.286 , pp. 291-1255
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.I.4
  • 10
    • 0034729685 scopus 로고    scopus 로고
    • Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex
    • Luo, Y. et al. Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex. Nature 405, 1073-1077 (2000).
    • (2000) Nature , vol.405 , pp. 1073-1077
    • Luo, Y.1
  • 11
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II protein secretion systems
    • Russel, M. Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J. Mol. Biol. 279, 485-499 (1998).
    • (1998) J. Mol. Biol. , vol.279 , pp. 485-499
    • Russel, M.1
  • 12
    • 0033612142 scopus 로고    scopus 로고
    • An aqueous channel for filamentous phage export
    • Marciano, D. K., Russel, M. & Simon, S. M. An aqueous channel for filamentous phage export. Science 284, 1516-1519 (1999).
    • (1999) Science , vol.284 , pp. 1516-1519
    • Marciano, D.K.1    Russel, M.2    Simon, S.M.3
  • 13
    • 0033033304 scopus 로고    scopus 로고
    • A new pathway for the secretion of virulence factors by bacteria: The flagellar export apparatus functions as a protein-secretion system
    • Young, G. M., Schmiel, D. H. & Miller, V. L. A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system. Proc. Natl. Acad Sci. USA 96, 6456-6461 (1999).
    • (1999) Proc. Natl. Acad Sci. USA , vol.96 , pp. 6456-6461
    • Young, G.M.1    Schmiel, D.H.2    Miller, V.L.3
  • 14
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • Kubori, T. et al. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280, 602-605 (1998).
    • (1998) Science , vol.280 , pp. 602-605
    • Kubori, T.1
  • 15
    • 0033230438 scopus 로고    scopus 로고
    • The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes
    • Blocker, A. et al. The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 147, 683-693 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 683-693
    • Blocker, A.1
  • 16
    • 0032522344 scopus 로고    scopus 로고
    • A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells
    • Knutton, S. et al. A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J. 17, 2166-2176 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2166-2176
    • Knutton, S.1
  • 17
    • 0033485823 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion-translocation system: Channel formation by secreted Yops
    • Tardy, F. et al. Yersinia enterocolitica type III secretion-translocation system: channel formation by secreted Yops. EMBO J. 18, 6793-6799 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6793-6799
    • Tardy, F.1
  • 18
    • 0034646722 scopus 로고    scopus 로고
    • Convergence of the secretory pathways for cholera toxin and the filamentous phage, CTXφ
    • Davis, B. M. et al. Convergence of the secretory pathways for cholera toxin and the filamentous phage, CTXφ. Science 288, 333-335 (2000).
    • (2000) Science , vol.288 , pp. 333-335
    • Davis, B.M.1
  • 19
    • 0031105945 scopus 로고    scopus 로고
    • Interactions between enteropathogenic Escherichia coli and host epithelial cells
    • Donnenberg, M. S., Kaper, J. B. & Finlay, B. B. Interactions between enteropathogenic Escherichia coli and host epithelial cells. Trends Microbiol. 5, 109-114 (1997).
    • (1997) Trends Microbiol. , vol.5 , pp. 109-114
    • Donnenberg, M.S.1    Kaper, J.B.2    Finlay, B.B.3
  • 20
    • 0032767933 scopus 로고    scopus 로고
    • The type IV bundle-forming pilus of enteropathogenic Escherichia coli undergoes dramatic alterations in structure associated with bacterial adherence, aggregation and dispersal
    • Knutton, S., Shaw, R. K., Anantha, R. P., Donnenberg, M. S. & Zorgani, A. A. The type IV bundle-forming pilus of enteropathogenic Escherichia coli undergoes dramatic alterations in structure associated with bacterial adherence, aggregation and dispersal. Mol. Microbiol. 33, 499-509 (1999).
    • (1999) Mol. Microbiol. , vol.33 , pp. 499-509
    • Knutton, S.1    Shaw, R.K.2    Anantha, R.P.3    Donnenberg, M.S.4    Zorgani, A.A.5
  • 21
    • 0031985046 scopus 로고    scopus 로고
    • The role of BfpF, a member of the PilT family of putative nucleotide-binding proteins, in type IV pilus biogenesis and in interactions between enteropathogenic Escherichia coli and host cells
    • Anantha, R. P., Stone, K. D. & Donnenberg, M. S. The role of BfpF, a member of the PilT family of putative nucleotide-binding proteins, in type IV pilus biogenesis and in interactions between enteropathogenic Escherichia coli and host cells. Infect. Immun. 66, 122-131 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 122-131
    • Anantha, R.P.1    Stone, K.D.2    Donnenberg, M.S.3
  • 22
    • 0032568984 scopus 로고    scopus 로고
    • Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli
    • Bieber, D. et al. Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli. Science 280, 2114-2118 (1998).
    • (1998) Science , vol.280 , pp. 2114-2118
    • Bieber, D.1
  • 23
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B. et al. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91, 511-520 (1997).
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1
  • 24
    • 0029737609 scopus 로고    scopus 로고
    • Novel form of actin-based motility transports bacteria on the surface of infected cells
    • Sanger, J. M., Chang, R., Ashton, F., Kaper, J. B. & Sanger, J. W. Novel form of actin-based motility transports bacteria on the surface of infected cells. Cell Motil. Cytoskeleton 34, 279-287 (1996).
    • (1996) Cell Motil. Cytoskeleton , vol.34 , pp. 279-287
    • Sanger, J.M.1    Chang, R.2    Ashton, F.3    Kaper, J.B.4    Sanger, J.W.5
  • 25
    • 0032974532 scopus 로고    scopus 로고
    • Rupture of the intestinal epithelial barrier and mucosal invasion by Shigella flexneri
    • Sansonetti, P. J., Tran, V. N. & Egile, C. Rupture of the intestinal epithelial barrier and mucosal invasion by Shigella flexneri. Clin. Infect. Dis. 28, 466-175 (1999).
    • (1999) Clin. Infect. Dis. , vol.28 , pp. 466-1175
    • Sansonetti, P.J.1    Tran, V.N.2    Egile, C.3
  • 27
    • 0028866712 scopus 로고
    • Actin-based motility of vaccinia virus
    • Cudmore, S., Cossart, P., Griffiths, G. & Way, M. Actin-based motility of vaccinia virus. Nature 378, 636-638 (1995).
    • (1995) Nature , vol.378 , pp. 636-638
    • Cudmore, S.1    Cossart, P.2    Griffiths, G.3    Way, M.4
  • 28
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel, T. P., Boujeman, R., Pantaloni, D. & Carlier, M. F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401, 613-616 (1999).
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujeman, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 29
    • 0031824696 scopus 로고    scopus 로고
    • Interactions of the invasive pathogens Salmonella typhimurium, Listeria monocytogenes and Shigella flexneri with M cells and murine Peyer's patches
    • Jensen, V. B., Harty, J. T. & Jones, B. D. Interactions of the invasive pathogens Salmonella typhimurium, Listeria monocytogenes and Shigella flexneri with M cells and murine Peyer's patches. Infect. Immun. 66, 3758-3766 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 3758-3766
    • Jensen, V.B.1    Harty, J.T.2    Jones, B.D.3
  • 30
    • 0029080233 scopus 로고
    • Role of interleukin-1 in the pathogenesis of experimental shigellosis
    • Sansonetti, P. J., Arondel, J., Cavaillon, J.-M. & Huerre, M. Role of interleukin-1 in the pathogenesis of experimental shigellosis. J. Clin. Invest. 96, 884-892 (1995).
    • (1995) J. Clin. Invest. , vol.96 , pp. 884-892
    • Sansonetti, P.J.1    Arondel, J.2    Cavaillon, J.-M.3    Huerre, M.4
  • 31
    • 0033598784 scopus 로고    scopus 로고
    • Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis
    • Achtman, M. et al. Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis. Proc. Natl Acad. Sci. USA 96, 14043-14048 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14043-14048
    • Achtman, M.1
  • 32
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G. R. & Wolf-Watz, H. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiol. 23, 861-867 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 33
    • 0031744367 scopus 로고    scopus 로고
    • Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice
    • Monack, D. M., Mecsas, J., Bouley, D. & Falkow, S. Yersinia-induced apoptosis in vivo aids in the establishment of a systemic infection of mice. J. Exp. Med. 188, 2127-2137 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 2127-2137
    • Monack, D.M.1    Mecsas, J.2    Bouley, D.3    Falkow, S.4
  • 34
    • 0033578311 scopus 로고    scopus 로고
    • Isolation of a temperate bacteriophage encoding the type III effector protein SopE from an epidemic Salmonella typhimurium strain
    • Mirold, S. et al. Isolation of a temperate bacteriophage encoding the type III effector protein SopE from an epidemic Salmonella typhimurium strain. Proc. Natl Acad. Sci. USA 96, 9845-9850 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9845-9850
    • Mirold, S.1
  • 35
    • 0033575956 scopus 로고    scopus 로고
    • A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu, Y. X. & Galán, J. E. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401, 293-297 (1999).
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.X.1    Galán, J.E.2
  • 36
    • 0033515032 scopus 로고    scopus 로고
    • The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1
    • Hersh, D. et al. The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. Proc. Natl Acad. Sci. USA 96, 2396-2401 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2396-2401
    • Hersh, D.1
  • 37
    • 0029117137 scopus 로고
    • Simultaneous identification of bacterial virulence genes by negative selection
    • Hensel, M. et al. Simultaneous identification of bacterial virulence genes by negative selection. Science 269, 400-403 (1995).
    • (1995) Science , vol.269 , pp. 400-403
    • Hensel, M.1
  • 38
    • 0034095005 scopus 로고    scopus 로고
    • Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase
    • Vazquez-Torres, A. et al. Salmonella pathogenicity island 2-dependent evasion of the phagocyte NADPH oxidase. Science 287, 1655-1658 (2000).
    • (2000) Science , vol.287 , pp. 1655-1658
    • Vazquez-Torres, A.1
  • 39
    • 0033565304 scopus 로고    scopus 로고
    • A Salmonella virulence protein that inhibits cellular trafficking
    • Uchiya, K. et al. A Salmonella virulence protein that inhibits cellular trafficking. EMBO J. 18, 3924-3933 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3924-3933
    • Uchiya, K.1
  • 40
    • 0033203232 scopus 로고    scopus 로고
    • Enteropathogenic E. coli acts through WASP and Arp2/3 complex to form actin pedestals
    • Kalman, D. et al. Enteropathogenic E. coli acts through WASP and Arp2/3 complex to form actin pedestals. Nature Cell Biol. 1, 389-391 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 389-391
    • Kalman, D.1
  • 41
    • 0032036390 scopus 로고    scopus 로고
    • Agents that inhibit Rho, Rac, and Cdc42 do not block formation of actin pedestals in HeLa cells infected with enteropathogenic Escherichia coli
    • Ben-Ami, G. et al. Agents that inhibit Rho, Rac, and Cdc42 do not block formation of actin pedestals in HeLa cells infected with enteropathogenic Escherichia coli. Infect. Immun. 66, 1755-1758 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 1755-1758
    • Ben-Ami, G.1
  • 42
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile, C. et al. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146, 1319-1332 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 1319-1332
    • Egile, C.1
  • 43
    • 0345593392 scopus 로고    scopus 로고
    • IpaC induces actin polymerization and filopodia formation during Shigella entry epithelial cells
    • Van Nhieu, G. T., Caron, E., Hall, A. & Sansonelti, P. J. IpaC induces actin polymerization and filopodia formation during Shigella entry epithelial cells. EMBO J. 18, 3249-3262 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3249-3262
    • Van Nhieu, G.T.1    Caron, E.2    Hall, A.3    Sansonelti, P.J.4
  • 44
    • 0030994387 scopus 로고    scopus 로고
    • Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin
    • Tran Van Nhieu, G., Ben-Ze'ev, A. & Sansonetti, P. J. Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin. EMBO J. 16, 2717-2729 (1997).
    • (1997) EMBO J. , vol.16 , pp. 2717-2729
    • Tran Van Nhieu, G.1    Ben-Ze'ev, A.2    Sansonetti, P.J.3
  • 45
    • 0344721483 scopus 로고    scopus 로고
    • Binding of the Shigella protein IpaA to vinculin induces F-actin depolymerization
    • Bourdet-Sicard, R. et al. Binding of the Shigella protein IpaA to vinculin induces F-actin depolymerization. EMBO J. 18, 5853-5862 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5853-5862
    • Bourdet-Sicard, R.1
  • 46
    • 0033621058 scopus 로고    scopus 로고
    • An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
    • Zhou, D. G., Mooseker, M. S. & Galán, J. E. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proc. Natl Acad. Sci. USA 96, 10176-10181 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10176-10181
    • Zhou, D.G.1    Mooseker, M.S.2    Galán, J.E.3
  • 47
    • 0033567985 scopus 로고    scopus 로고
    • Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella
    • Hayward, R. D. & Koronakis, V. Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella. EMBO J. 18, 4926-4934 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4926-4934
    • Hayward, R.D.1    Koronakis, V.2
  • 48
    • 0032577563 scopus 로고    scopus 로고
    • S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R. & Galán, J. E. S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826 (1998).
    • (1998) Cell , vol.93 , pp. 815-826
    • Hardt, W.D.1    Chen, L.M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galán, J.E.5
  • 49
    • 0031780201 scopus 로고    scopus 로고
    • YopI of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-α production and downregulation of the MAP kinases p38 and JNK
    • Palmer, L. E., Hobbie, S., Galán, J. E. & Bliska, J. B. YopI of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-α production and downregulation of the MAP kinases p38 and JNK. Mol. Microbiol. 27, 953-965 (1998).
    • (1998) Mol. Microbiol. , vol.27 , pp. 953-965
    • Palmer, L.E.1    Hobbie, S.2    Galán, J.E.3    Bliska, J.B.4
  • 50
    • 0031775572 scopus 로고    scopus 로고
    • The yopI locus is required for Yersinia-mediated inhibition of NF-κB activation and cytokine expression: YopI contains a eukaryolic SH2-like domain that is essential for its repressive activity
    • Schesser, K. et al. The yopI locus is required for Yersinia-mediated inhibition of NF-κB activation and cytokine expression: YopI contains a eukaryolic SH2-like domain that is essential for its repressive activity. Mol. Microbiol. 28, 1067-1079 (1998).
    • (1998) Mol. Microbiol. , vol.28 , pp. 1067-1079
    • Schesser, K.1
  • 51
    • 0032801539 scopus 로고    scopus 로고
    • Localization of the Yersinia PTPase to focal complexes is an important virulence mechanism
    • Persson, C. et al. Localization of the Yersinia PTPase to focal complexes is an important virulence mechanism. Mol. Microbiol. 33, 828-838 (1999).
    • (1999) Mol. Microbiol. , vol.33 , pp. 828-838
    • Persson, C.1
  • 52
    • 0030913232 scopus 로고    scopus 로고
    • Gas as a substrate Yersinia YopH (Yop54), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • Gas as a substrate Yersinia YopH (Yop54), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 16, 2730-2744 (1997).
    • (1997) EMBO J. , vol.16 , pp. 2730-2744
    • Black, D.S.1    Bliska, J.H.2
  • 53
    • 0030978909 scopus 로고    scopus 로고
    • Gas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
    • Gas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions. EMBO J. 16, 2307-2318 (1997).
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1    Carballeira, N.2    Wolf-Watz, H.3    Fällman, M.4
  • 54
    • 0032829693 scopus 로고    scopus 로고
    • The cytotoxin YopT of Yersinia enterocolitica induces modification and cellular redistribution of the small GTP-binding protein RhoA
    • Zumbihl, R. et al. The cytotoxin YopT of Yersinia enterocolitica induces modification and cellular redistribution of the small GTP-binding protein RhoA. J. Biol. Chem. 274, 29289-29293 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 29289-29293
    • Zumbihl, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.