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0027819033
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Molecular mechanisms of cell and tissue invasion by Shigella flexneri
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Sansonetti PJ Molecular mechanisms of cell and tissue invasion by Shigella flexneri. Infect Agents Dis. 2:1993;201-206.
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Infect Agents Dis
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Sansonetti, P.J.1
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0030032027
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Invasion and the pathogenesis of Shigella infections
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V.L. Miller. Berlin: Springer Verlag
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Parsot C, Sansonetti PJ Invasion and the pathogenesis of Shigella infections. Miller VL Bacterial Invasiveness. 1996;25-42 Springer Verlag, Berlin.
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(1996)
Bacterial Invasiveness
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Parsot, C.1
Sansonetti, P.J.2
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3
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0031864184
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Type III secretion systems in bacterial pathogens of animals and plants
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An extensive and comprehensive review describing parallels and differences of type III secretion systems in plant and animal pathogens
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Hueck CJ Type III secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev. 62:1998;379-433. An extensive and comprehensive review describing parallels and differences of type III secretion systems in plant and animal pathogens.
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Microbiol Mol Biol Rev
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Hueck, C.J.1
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4
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0031026828
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The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
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A review describing the complex regulation as well as the role of translocated Yop proteins of the Yersinia Ysc type III secretion apparatus, which has been the most studied to date
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Cornelis G, Wolf-Watz H The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol Microbiol. 23:1997;861-867. A review describing the complex regulation as well as the role of translocated Yop proteins of the Yersinia Ysc type III secretion apparatus, which has been the most studied to date.
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Mol Microbiol
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Cornelis, G.1
Wolf-Watz, H.2
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5
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0032522344
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A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells
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This paper describes a filamentous organelle, reminiscent of the Salmonella invasomes, which appears at the surface of enteropathogenic E. coli (EPEC) upon cultivation in cell medium, and forms a link between the bacterium and the host cell membrane. These EspA-containing filaments are required for translocation of EPEC proteins into the host cell cytosol during the early phases of formation of attaching/effacing lesions
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Knutton S, Rosenshine I, Pallen MJ, Nisan I, Neves BC, Bain C, Wolff C, Dougan G, Frankel G A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J. 17:1998;2166-2176. This paper describes a filamentous organelle, reminiscent of the Salmonella invasomes, which appears at the surface of enteropathogenic E. coli (EPEC) upon cultivation in cell medium, and forms a link between the bacterium and the host cell membrane. These EspA-containing filaments are required for translocation of EPEC proteins into the host cell cytosol during the early phases of formation of attaching/effacing lesions.
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EMBO J
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Knutton, S.1
Rosenshine, I.2
Pallen, M.J.3
Nisan, I.4
Neves, B.C.5
Bain, C.6
Wolff, C.7
Dougan, G.8
Frankel, G.9
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6
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0032562678
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Supramolecular structure of the Salmonella typhimurium type III protein secretion
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Flagellar structures containing components of the Salmonella type III secretetion apparatus are visualized by electron microspcopy on the bacterial surface, and may represent the 'needle' that allows translocation of Salmonella effectors into host cell
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Kubori T, Matsushima Y, Nakamura D, Uralil J, Lara-Tejero M, Sukhan A, Galan JE, Aizawa SI Supramolecular structure of the Salmonella typhimurium type III protein secretion. Science. 280:1998;602-605. Flagellar structures containing components of the Salmonella type III secretetion apparatus are visualized by electron microspcopy on the bacterial surface, and may represent the 'needle' that allows translocation of Salmonella effectors into host cell.
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Science
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Kubori, T.1
Matsushima, Y.2
Nakamura, D.3
Uralil, J.4
Lara-Tejero, M.5
Sukhan, A.6
Galan, J.E.7
Aizawa, S.I.8
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7
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0029731661
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Cross-talk between bacterial pathogens and their host cells
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Galan JE, Bliska JB Cross-talk between bacterial pathogens and their host cells. Annu Rev Cell Dev Biol. 12:1996;221-255.
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Galan, J.E.1
Bliska, J.B.2
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8
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0031018478
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Secretion of Shigella flexneri Ipa invasins on contact with epithelial cells and subsequent entry of the bacterium into cells are growth stage dependent
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Mounier J, Bahrani F, Sansonetti PJ Secretion of Shigella flexneri Ipa invasins on contact with epithelial cells and subsequent entry of the bacterium into cells are growth stage dependent. Infect Immun. 65:1997;774-782.
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Infect Immun
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Mounier, J.1
Bahrani, F.2
Sansonetti, P.J.3
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9
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0029039881
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Contact of Shigella with host cells triggers release of Ipa invasins and is an essential function of invasiveness
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Watarai M, Tobe T, Yoshikawa M, Sasakawa C Contact of Shigella with host cells triggers release of Ipa invasins and is an essential function of invasiveness. EMBO J. 14:1995;2461-2470.
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EMBO J
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Watarai, M.1
Tobe, T.2
Yoshikawa, M.3
Sasakawa, C.4
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10
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0027982852
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Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
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Rosqvist R, Magnusson KE, Wolf-Watz H Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13:1994;964-972.
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Rosqvist, R.1
Magnusson, K.E.2
Wolf-Watz, H.3
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11
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0028072943
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The secretion of the Shigella flexneri Ipa invasins is induced by the epithelial cell and controlled by IpaB and IpaD
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Ménard R, Sansonetti PJ, Parsot C The secretion of the Shigella flexneri Ipa invasins is induced by the epithelial cell and controlled by IpaB and IpaD. EMBO J. 13:1994;5293-5302.
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EMBO J
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Ménard, R.1
Sansonetti, P.J.2
Parsot, C.3
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12
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0030032067
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The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells
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Ménard R, Prévost MC, Gounon P, Sansonetti PJ, Dehio C The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells. Proc Natl Acad Sci USA. 93:1996;1254-1258.
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Proc Natl Acad Sci USA
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Ménard, R.1
Prévost, M.C.2
Gounon, P.3
Sansonetti, P.J.4
Dehio, C.5
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13
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0029915666
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Interaction of Ipa proteins of Shigella flexneri with alpha5-beta1 integrin promotes entry of the bacteria into mammalian cells
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Watarai M, Funato S, Sasakawa C Interaction of Ipa proteins of Shigella flexneri with alpha5-beta1 integrin promotes entry of the bacteria into mammalian cells. J Exp Med. 183:1996;991-999.
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J Exp Med
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Watarai, M.1
Funato, S.2
Sasakawa, C.3
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14
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0030015626
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Rho-dependent membrane folding causes Shigella entry into epithelial cells
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Adam T, Giry M, Boquet P, Sansonetti P Rho-dependent membrane folding causes Shigella entry into epithelial cells. EMBO J. 15:1996;3315-3321.
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EMBO J
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Adam, T.1
Giry, M.2
Boquet, P.3
Sansonetti, P.4
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15
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0031052018
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Rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells
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Watarai M, Kamata Y, Kozaki S, Sasakawa C Rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells. J Exp Med. 185:1997;281-292.
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J Exp Med
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Watarai, M.1
Kamata, Y.2
Kozaki, S.3
Sasakawa, C.4
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16
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0028229539
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ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
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Tsukita S, Oishi K, Sato N, Sagara J, Kawai A, Tsukita S ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol. 126:1994;391-401.
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Tsukita, S.1
Oishi, K.2
Sato, N.3
Sagara, J.4
Kawai, A.5
Tsukita, S.6
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17
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0029943112
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Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5 biphosphate
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Gilmore AP, Burridge K Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5 biphosphate. Nature. 381:1996;531-535.
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Nature
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Gilmore, A.P.1
Burridge, K.2
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0030846295
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Direct interaction of the RhoGDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
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Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Tsukita S, Takai Y Direct interaction of the RhoGDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J Biol Chem. 272:1997;23371-23375.
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J Biol Chem
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Takahashi, K.1
Sasaki, T.2
Mammoto, A.3
Takaishi, K.4
Kameyama, T.5
Tsukita, S.6
Tsukita, S.7
Takai, Y.8
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19
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0030994387
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Modulation of bacterial entry into epithelial cells by interaction between vinculin and the Shigella IpaA invasin
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It is shown that the Shigella IpaA protein binds to vinculin and favors bacterial internalization by allowing the formation of a adhesion-like structure. Shigella internalization still occurrs at low levels in the absence of IpaA, suggesting the existence of different bacterial effectors that act in concert to promote bacterial entry
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Tran Van Nhieu G, Ben Ze'ev A, Sansonetti PJ Modulation of bacterial entry into epithelial cells by interaction between vinculin and the Shigella IpaA invasin. EMBO J. 16:1997;2717-2729. It is shown that the Shigella IpaA protein binds to vinculin and favors bacterial internalization by allowing the formation of a adhesion-like structure. Shigella internalization still occurrs at low levels in the absence of IpaA, suggesting the existence of different bacterial effectors that act in concert to promote bacterial entry.
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(1997)
EMBO J
, vol.16
, pp. 2717-2729
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Tran Van Nhieu, G.1
Ben Ze'Ev, A.2
Sansonetti, P.J.3
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20
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0028961293
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Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
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Nobes CD, Hall A Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
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Cell
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Nobes, C.D.1
Hall, A.2
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22
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0032577563
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S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
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Salmonella entry into epithelial cells was shown to require activation of the small GTPases Cdc42 and Rac. It is reported in this paper that SopE, a Salmonella protein that is translocated into the cytosol of host cells, can act as an exchange factor for Cdc42 and Rac, thus inducing cellular rufflings required for bacterial uptake. SopE, however, may not be sufficient to promote efficient bacterial uptake, and other Salmonella effectors are probably simultaneously modulating the entry process
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Hardt W-D, Chen L-M, Schuebel KE, Bustelo XR, Galan J S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell. 93:1998;815-826. Salmonella entry into epithelial cells was shown to require activation of the small GTPases Cdc42 and Rac. It is reported in this paper that SopE, a Salmonella protein that is translocated into the cytosol of host cells, can act as an exchange factor for Cdc42 and Rac, thus inducing cellular rufflings required for bacterial uptake. SopE, however, may not be sufficient to promote efficient bacterial uptake, and other Salmonella effectors are probably simultaneously modulating the entry process.
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(1998)
Cell
, vol.93
, pp. 815-826
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Hardt, W.-D.1
Chen, L.-M.2
Schuebel, K.E.3
Bustelo, X.R.4
Galan, J.5
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23
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0032539017
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Interferon-alpha inhibits a Src-mediated pathway necessary for Shigella-induced cytoskeletal rearrangements during entry into epithelial cells
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Interferon α and β were known to specifically inhibit Shigella but not Salmonella uptake by epithelial cells. This paper reports that Shigella require activation of the Src tyrosine kinase to induce cytoskeletal rearrangements during entry, and that interferon impairs Shigella-mediated Src activation. The data also implicate a dual role for Src, in the induction of Shigella-induced foci of actin polymerization, and also in the down-regulation of these foci
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Duménil G, Olivo J-C, Pellegrini S, Fellous M, Sansonetti PJ, Tran Van Nhieu G Interferon-alpha inhibits a Src-mediated pathway necessary for Shigella-induced cytoskeletal rearrangements during entry into epithelial cells. J Cell Biol. 143:1998;1003-1012. Interferon α and β were known to specifically inhibit Shigella but not Salmonella uptake by epithelial cells. This paper reports that Shigella require activation of the Src tyrosine kinase to induce cytoskeletal rearrangements during entry, and that interferon impairs Shigella-mediated Src activation. The data also implicate a dual role for Src, in the induction of Shigella-induced foci of actin polymerization, and also in the down-regulation of these foci.
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(1998)
J Cell Biol
, vol.143
, pp. 1003-1012
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Duménil, G.1
Olivo, J.-C.2
Pellegrini, S.3
Fellous, M.4
Sansonetti, P.J.5
Tran Van Nhieu, G.6
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