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Volumn 449, Issue 7164, 2007, Pages 862-866

Helicobacter exploits integrin for type IV secretion and kinase activation

Author keywords

[No Author keywords available]

Indexed keywords

FOCAL ADHESION KINASE; INTEGRIN; PHOSPHOTRANSFERASE; PROTEIN TYROSINE KINASE;

EID: 35349031591     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06187     Document Type: Article
Times cited : (520)

References (24)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687 (2002).
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra, S. K. & Schlaepfer, D. D. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18, 516-523 (2006).
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 3
    • 0029775681 scopus 로고    scopus 로고
    • Ruoslahti, E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12, 697-715 (1996).
    • Ruoslahti, E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12, 697-715 (1996).
  • 4
    • 0004014992 scopus 로고    scopus 로고
    • Eble, J. A. & Kühn, K, eds, Springer, Heidelberg
    • Eble, J. A. & Kühn, K. (eds) Integrin-Ligand Interaction (Springer, Heidelberg, 1997).
    • (1997) Integrin-Ligand Interaction
  • 5
    • 23444447782 scopus 로고
    • Binding and internalization of microorganisms by integrin-receptors
    • Isberg, R. R. & Tran Van Nhieu, G. Binding and internalization of microorganisms by integrin-receptors. Trends Microbiol. 2, 10-14 (1994).
    • (1994) Trends Microbiol , vol.2 , pp. 10-14
    • Isberg, R.R.1    Tran Van Nhieu, G.2
  • 6
    • 0025250067 scopus 로고
    • Multiple β1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells
    • Isberg, R. R. & Leong, J. M. Multiple β1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell 60, 861-871 (1990).
    • (1990) Cell , vol.60 , pp. 861-871
    • Isberg, R.R.1    Leong, J.M.2
  • 7
    • 0141756140 scopus 로고    scopus 로고
    • Bacterial pathogenesis: Exploiting cellular adherence
    • Boyle, E. C. & Finlay, B. B. Bacterial pathogenesis: exploiting cellular adherence. Curr. Opin. Cell Biol. 15, 633-639 (2003).
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 633-639
    • Boyle, E.C.1    Finlay, B.B.2
  • 8
    • 1842456892 scopus 로고    scopus 로고
    • The versatile bacterial type IV-secretion systems
    • Cascales, E. & Christie, P. J. The versatile bacterial type IV-secretion systems. Nature Rev. Microbiol. 1, 137-149 (2003).
    • (2003) Nature Rev. Microbiol , vol.1 , pp. 137-149
    • Cascales, E.1    Christie, P.J.2
  • 9
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • Backert, S. & Meyer, T. F. Type IV secretion systems and their effectors in bacterial pathogenesis. Curr. Opin. Microbiol. 9, 207-217 (2006).
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 10
    • 0038780624 scopus 로고    scopus 로고
    • Disruption of the epithelial apical-junctional complex by Helicobacter pylori CagA
    • Amieva, M. R. et al. Disruption of the epithelial apical-junctional complex by Helicobacter pylori CagA. Science 300, 1430-1434 (2004).
    • (2004) Science , vol.300 , pp. 1430-1434
    • Amieva, M.R.1
  • 11
    • 0036370334 scopus 로고    scopus 로고
    • Helicobacter pylori and gastrointestinal tract adenocarcinomas
    • Peek, R. M. Jr & Blaser, M. J. Helicobacter pylori and gastrointestinal tract adenocarcinomas. Nature Rev. Cancer 2, 28-36 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 28-36
    • Peek Jr, R.M.1    Blaser, M.J.2
  • 12
    • 0034695879 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated bacterial proteins: Trojan horses for the host cell
    • Covacci, A. & Rappuoli, R. Tyrosine-phosphorylated bacterial proteins: Trojan horses for the host cell. J. Exp. Med. 191, 587-592 (2000).
    • (2000) J. Exp. Med , vol.191 , pp. 587-592
    • Covacci, A.1    Rappuoli, R.2
  • 13
    • 34247185194 scopus 로고    scopus 로고
    • The role of Helicobacter pylori CagA in gastric carcinogenesis
    • Hatakeyama, M. The role of Helicobacter pylori CagA in gastric carcinogenesis. Int. J. Hematol. 84, 301-308 (2006).
    • (2006) Int. J. Hematol , vol.84 , pp. 301-308
    • Hatakeyama, M.1
  • 14
    • 0035162820 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 972 of the Helicobacter pylori CagA protein is essential for induction of a scattering phenotype in gastric epithelial cells
    • Backert, S. et al. Phosphorylation of tyrosine 972 of the Helicobacter pylori CagA protein is essential for induction of a scattering phenotype in gastric epithelial cells. Mol. Microbiol. 42, 631-644 (2001).
    • (2001) Mol. Microbiol , vol.42 , pp. 631-644
    • Backert, S.1
  • 15
    • 0029671372 scopus 로고    scopus 로고
    • β1 integrin-dependent and-independent polymerization of fibronectin
    • Wennerberg, K. et al. β1 integrin-dependent and-independent polymerization of fibronectin. J. Cell Biol. 132, 227-238 (1996).
    • (1996) J. Cell Biol , vol.132 , pp. 227-238
    • Wennerberg, K.1
  • 16
    • 0038046757 scopus 로고    scopus 로고
    • A novel sheathed surface organelle of the H .pylori cag-type IV-secretion system
    • Rohde, M. et al. A novel sheathed surface organelle of the H .pylori cag-type IV-secretion system. Mol. Microbiol. 49, 219-234 (2003).
    • (2003) Mol. Microbiol , vol.49 , pp. 219-234
    • Rohde, M.1
  • 17
    • 0037178771 scopus 로고    scopus 로고
    • Helicobacter pylori SabA-adhesin in persistent infection and chronic inflammation
    • Mahdavi, J. et al. Helicobacter pylori SabA-adhesin in persistent infection and chronic inflammation. Science 297, 573-578 (2002).
    • (2002) Science , vol.297 , pp. 573-578
    • Mahdavi, J.1
  • 18
    • 3242748894 scopus 로고    scopus 로고
    • Functional adaptation of BabA, the H. pylori ABO-blood group antigen binding adhesin
    • Aspholm-Hurtig, M. et al. Functional adaptation of BabA, the H. pylori ABO-blood group antigen binding adhesin. Science 305, 519-522 (2004).
    • (2004) Science , vol.305 , pp. 519-522
    • Aspholm-Hurtig, M.1
  • 19
    • 0032528956 scopus 로고    scopus 로고
    • Selective increase of the permeability of polarized epithelial cell monolayers by Helicobacter pylori vacuolating toxin
    • Papini, E. et al. Selective increase of the permeability of polarized epithelial cell monolayers by Helicobacter pylori vacuolating toxin. J. Clin. Invest. 102, 813-820 (1998).
    • (1998) J. Clin. Invest , vol.102 , pp. 813-820
    • Papini, E.1
  • 20
    • 0036130660 scopus 로고    scopus 로고
    • Specific entry of Helicobacter pylori into cultured gastric epithelial cells via a zipper-like mechanism
    • Kwok, T. et al. Specific entry of Helicobacter pylori into cultured gastric epithelial cells via a zipper-like mechanism. Infect. Immun. 70, 2108-2120 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 2108-2120
    • Kwok, T.1
  • 21
    • 0036510363 scopus 로고    scopus 로고
    • Src is the kinase of the Helicobacter pylori CagA protein in vitro and in vivo
    • Selbach, M. et al. Src is the kinase of the Helicobacter pylori CagA protein in vitro and in vivo. J. Biol. Chem. 277, 6775-6778 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 6775-6778
    • Selbach, M.1
  • 22
    • 21144452845 scopus 로고    scopus 로고
    • 1 antagonists: Biological evaluation using cell adhesion assay and surface plasmon resonance
    • 1 antagonists: Biological evaluation using cell adhesion assay and surface plasmon resonance. ChemBioChem 6, 272-276 (2005).
    • (2005) ChemBioChem , vol.6 , pp. 272-276
    • Zimmermann, D.1
  • 23
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C. Jr. Protein secondary structure and circular dichroism: a practical guide. Proteins 7, 205-214 (1990).
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 24
    • 0032493657 scopus 로고    scopus 로고
    • The involvement of the fibronectin type II-like modules of human gelatinase A in cell surface localization and activation
    • Steffensen, B. et al. The involvement of the fibronectin type II-like modules of human gelatinase A in cell surface localization and activation. J. Biol. Chem. 273, 20622-20628 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 20622-20628
    • Steffensen, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.