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Volumn 10, Issue 12, 2000, Pages 735-738

Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with α-actinin

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

EID: 0034659385     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00543-1     Document Type: Article
Times cited : (112)

References (14)
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    • Kenny, B.1    Devinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 2
    • 0032882799 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli translocated intimin receptor, Tir, requires a specific chaperone for stable secretion
    • Abe A., de Grado M., Pfuetzner R.A., Sanchez-Sanmartin C., Devinney R., Puente J.L.et al. Enteropathogenic Escherichia coli translocated intimin receptor, Tir, requires a specific chaperone for stable secretion. Mol Microbiol. 33:1999;1162-1175.
    • (1999) Mol Microbiol , vol.33 , pp. 1162-1175
    • Abe, A.1    De Grado, M.2    Pfuetzner, R.A.3    Sanchez-Sanmartin, C.4    Devinney, R.5    Puente, J.L.6
  • 3
    • 0033002855 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia coli (EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications
    • Kenny B. Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia coli (EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications. Mol Microbiol. 31:1999;1229-1241.
    • (1999) Mol Microbiol , vol.31 , pp. 1229-1241
    • Kenny, B.1
  • 5
    • 0032407404 scopus 로고    scopus 로고
    • Intracellular pathogens and the actin cytoskeleton
    • Dramsi S., Cossart P. Intracellular pathogens and the actin cytoskeleton. Annu Rev Cell Dev Biol. 14:1998;137-166.
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    • Putting E. coli on a pedestal: A unique system to study signal transduction and the actin cytoskeleton
    • Goosney D.L., de Grado M., Finlay B.B. Putting E. coli on a pedestal: a unique system to study signal transduction and the actin cytoskeleton. Trends Cell Biol. 9:1999;11-14.
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    • Goosney, D.L.1    De Grado, M.2    Finlay, B.B.3
  • 8
    • 0029737609 scopus 로고    scopus 로고
    • Novel form of actin-based motility transports bacteria on the surfaces 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 surfaces of infected cells. Cell Motil Cytoskeleton. 34:1996;279-287.
    • (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
  • 10
    • 0025291522 scopus 로고
    • : An interaction between alpha-actinin and the beta 1 integrin subunit in vitro
    • Otey C.A., Pavalko F.M., Burridge K. : An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. J Cell Biol. 111:1990;721-729.
    • (1990) J Cell Biol , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 11
    • 0028822996 scopus 로고
    • Molecular characterization of a carboxy-terminal eukaryotic-cell-binding domain of intimin from enteropathogenic Escherichia coli
    • Frankel G., Candy D.C., Fabiani E., Adu-Bobie J., Gil S., Novakova M.et al. Molecular characterization of a carboxy-terminal eukaryotic-cell-binding domain of intimin from enteropathogenic Escherichia coli. Infect Immun. 63:1995;4323-4328.
    • (1995) Infect Immun , vol.63 , pp. 4323-4328
    • Frankel, G.1    Candy, D.C.2    Fabiani, E.3    Adu-Bobie, J.4    Gil, S.5    Novakova, M.6
  • 12
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    • Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells
    • Isberg R.R., Leong J.M. Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell. 60:1990;861-871.
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  • 13
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    • The cell-binding domain of intimin from enteropathogenic Escherichia coli binds to beta1 integrins
    • Frankel G., Lider O., Hershkoviz R., Mould A.P., Kachalsky S.G., Candy D.C.A.et al. The cell-binding domain of intimin from enteropathogenic Escherichia coli binds to beta1 integrins. J Biol Chem. 271:1996;20359-20364.
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  • 14
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    • : Beta1-chain integrins are not essential for intimin-mediated host cell attachment and enteropathogenic Escherichia coli-induced actin condensation
    • Liu H., Magoun L., Leong J.M. : Beta1-chain integrins are not essential for intimin-mediated host cell attachment and enteropathogenic Escherichia coli-induced actin condensation. Infect Immun. 67:1999;2045-2049.
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    • Liu, H.1    Magoun, L.2    Leong, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.