메뉴 건너뛰기




Volumn 33, Issue 2, 2008, Pages 80-90

Emerging roles of Abl family tyrosine kinases in microbial pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; ACTIN; BACTERIAL PROTEIN; TYROSINE; VIRUS PROTEIN;

EID: 38949197397     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2007.10.006     Document Type: Review
Times cited : (61)

References (75)
  • 1
    • 28844508817 scopus 로고    scopus 로고
    • Leukemic kinases of the Abl family - an update
    • Voss J., et al. Leukemic kinases of the Abl family - an update. Signal Trans. 1 (2001) 1-26
    • (2001) Signal Trans. , vol.1 , pp. 1-26
    • Voss, J.1
  • 2
    • 0038445642 scopus 로고    scopus 로고
    • Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases
    • Woodring P.J., et al. Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases. J. Cell Sci. 116 (2003) 2613-2626
    • (2003) J. Cell Sci. , vol.116 , pp. 2613-2626
    • Woodring, P.J.1
  • 3
    • 0346496472 scopus 로고    scopus 로고
    • How do Abl family kinases regulate cell shape and movement?
    • Hernandez S.E., et al. How do Abl family kinases regulate cell shape and movement?. Trends Cell Biol. 14 (2004) 36-44
    • (2004) Trends Cell Biol. , vol.14 , pp. 36-44
    • Hernandez, S.E.1
  • 4
  • 5
    • 38949127655 scopus 로고    scopus 로고
    • Regulation of Abl kinases by adaptor proteins
    • Shishido T., and Suzuki J. Regulation of Abl kinases by adaptor proteins. Gene Ther. Mol. Biol. 9 (2005) 339-342
    • (2005) Gene Ther. Mol. Biol. , vol.9 , pp. 339-342
    • Shishido, T.1    Suzuki, J.2
  • 6
    • 0344626925 scopus 로고    scopus 로고
    • A myristoyl/phosphotyrosine switch regulates c-Abl
    • Hantschel O., et al. A myristoyl/phosphotyrosine switch regulates c-Abl. Cell 112 (2003) 845-857
    • (2003) Cell , vol.112 , pp. 845-857
    • Hantschel, O.1
  • 7
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar B., et al. Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 112 (2003) 859-871
    • (2003) Cell , vol.112 , pp. 859-871
    • Nagar, B.1
  • 8
    • 0037384252 scopus 로고    scopus 로고
    • A new link between the c-Abl tyrosine kinase and phosphoinositide signalling through PLC-gamma1
    • Plattner R., et al. A new link between the c-Abl tyrosine kinase and phosphoinositide signalling through PLC-gamma1. Nat. Cell Biol. 5 (2003) 309-319
    • (2003) Nat. Cell Biol. , vol.5 , pp. 309-319
    • Plattner, R.1
  • 9
    • 0037508877 scopus 로고    scopus 로고
    • Two distinct phosphorylation pathways have additive effects on Abl family kinase activation
    • Tanis K.Q., et al. Two distinct phosphorylation pathways have additive effects on Abl family kinase activation. Mol. Cell. Biol. 23 (2003) 3884-3896
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3884-3896
    • Tanis, K.Q.1
  • 10
    • 0037459341 scopus 로고    scopus 로고
    • Variation on an Src-like theme
    • Harrison S.C. Variation on an Src-like theme. Cell 112 (2003) 737-740
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 11
    • 0033568349 scopus 로고    scopus 로고
    • c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF
    • Plattner R., et al. c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13 (1999) 2400-2411
    • (1999) Genes Dev. , vol.13 , pp. 2400-2411
    • Plattner, R.1
  • 12
    • 0030459950 scopus 로고    scopus 로고
    • Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic-nuclear transport
    • Lewis J.M., et al. Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic-nuclear transport. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 15174-15179
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 15174-15179
    • Lewis, J.M.1
  • 13
    • 0032486386 scopus 로고    scopus 로고
    • Integrins regulate the association and phosphorylation of paxillin by c-Abl
    • Lewis J.M., and Schwartz M.A. Integrins regulate the association and phosphorylation of paxillin by c-Abl. J. Biol. Chem. 273 (1998) 14225-14230
    • (1998) J. Biol. Chem. , vol.273 , pp. 14225-14230
    • Lewis, J.M.1    Schwartz, M.A.2
  • 14
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mighter B.J., et al. Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr. Biol. 5 (1995) 296-305
    • (1995) Curr. Biol. , vol.5 , pp. 296-305
    • Mighter, B.J.1
  • 15
    • 0028243505 scopus 로고
    • c-Abl kinase regulates the protein binding activity of c-Crk
    • Feller S.M., et al. c-Abl kinase regulates the protein binding activity of c-Crk. EMBO J. 13 (1994) 2341-2351
    • (1994) EMBO J. , vol.13 , pp. 2341-2351
    • Feller, S.M.1
  • 16
    • 0035475308 scopus 로고    scopus 로고
    • Crk family adaptors-signalling complex formation and biological roles
    • Feller S.M. Crk family adaptors-signalling complex formation and biological roles. Oncogene 20 (2001) 6348-6371
    • (2001) Oncogene , vol.20 , pp. 6348-6371
    • Feller, S.M.1
  • 17
    • 34249902061 scopus 로고    scopus 로고
    • Structural basis for the transforming activity of human cancer-related signalling adaptor protein CRK
    • Kobashigawa Y., et al. Structural basis for the transforming activity of human cancer-related signalling adaptor protein CRK. Nat. Struct. Mol. Biol. 14 (2007) 503-510
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 503-510
    • Kobashigawa, Y.1
  • 18
    • 33845986367 scopus 로고    scopus 로고
    • c-Abl interacts with the WAVE2 signalling complex to induce membrane ruffling and cell spreading
    • Stuart J.R., et al. c-Abl interacts with the WAVE2 signalling complex to induce membrane ruffling and cell spreading. J. Biol. Chem. 281 (2006) 31290-31297
    • (2006) J. Biol. Chem. , vol.281 , pp. 31290-31297
    • Stuart, J.R.1
  • 19
    • 12844251861 scopus 로고    scopus 로고
    • Abelson-interactor-1 promotes WAVE2 membrane translocation and Abelson-mediated tyrosine phosphorylation required for WAVE2 activation
    • Leng Y., et al. Abelson-interactor-1 promotes WAVE2 membrane translocation and Abelson-mediated tyrosine phosphorylation required for WAVE2 activation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1098-1103
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1098-1103
    • Leng, Y.1
  • 20
    • 26444452643 scopus 로고    scopus 로고
    • Abl kinases regulate actin comet tail elongation via an N-WASP-dependent pathway
    • Burton E.A., et al. Abl kinases regulate actin comet tail elongation via an N-WASP-dependent pathway. Mol. Cell. Biol. 25 (2005) 8834-8843
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8834-8843
    • Burton, E.A.1
  • 21
    • 30844466190 scopus 로고    scopus 로고
    • Protein complexes regulating Arp2/3-mediated actin assembly
    • Stradal T.E., and Scita G. Protein complexes regulating Arp2/3-mediated actin assembly. Curr. Opin. Cell Biol. 18 (2006) 4-10
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 4-10
    • Stradal, T.E.1    Scita, G.2
  • 22
    • 0142041888 scopus 로고    scopus 로고
    • Abl tyrosine kinases are required for infection by Shigella flexneri
    • Burton E.A., et al. Abl tyrosine kinases are required for infection by Shigella flexneri. EMBO J. 22 (2003) 5471-5479
    • (2003) EMBO J. , vol.22 , pp. 5471-5479
    • Burton, E.A.1
  • 23
    • 33746098167 scopus 로고    scopus 로고
    • The Caenorhabditis elegans ABL-1 tyrosine kinase is required for Shigella flexneri pathogenesis
    • Burton E.A., et al. The Caenorhabditis elegans ABL-1 tyrosine kinase is required for Shigella flexneri pathogenesis. Appl. Environ. Microbiol. 72 (2006) 5043-5051
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5043-5051
    • Burton, E.A.1
  • 24
    • 13444263489 scopus 로고    scopus 로고
    • Tyrosine kinase signalling and type III effectors orchestrating Shigella invasion
    • Nhieu G.T., et al. Tyrosine kinase signalling and type III effectors orchestrating Shigella invasion. Curr. Opin. Microbiol. 8 (2005) 16-20
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 16-20
    • Nhieu, G.T.1
  • 25
    • 0029005239 scopus 로고
    • Invasion of epithelial cells by Shigella flexneri induces tyrosine phosphorylation of cortactin by a pp60c-src-mediated signalling pathway
    • Dehio C., et al. Invasion of epithelial cells by Shigella flexneri induces tyrosine phosphorylation of cortactin by a pp60c-src-mediated signalling pathway. EMBO J. 14 (1995) 2471-2482
    • (1995) EMBO J. , vol.14 , pp. 2471-2482
    • Dehio, C.1
  • 26
    • 16244370694 scopus 로고    scopus 로고
    • Cortactin: an Achilles' heel of the actin cytoskeleton targeted by pathogens
    • Selbach M., and Backert S. Cortactin: an Achilles' heel of the actin cytoskeleton targeted by pathogens. Trends Microbiol. 13 (2005) 181-189
    • (2005) Trends Microbiol. , vol.13 , pp. 181-189
    • Selbach, M.1    Backert, S.2
  • 27
    • 33847284434 scopus 로고    scopus 로고
    • A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation
    • Boyle S.N., et al. A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation. Curr. Biol. 17 (2007) 445-451
    • (2007) Curr. Biol. , vol.17 , pp. 445-451
    • Boyle, S.N.1
  • 28
    • 3342951789 scopus 로고    scopus 로고
    • Cortactin and Crk cooperate to trigger actin polymerization during Shigella invasion of epithelial cells
    • Bougneres L., et al. Cortactin and Crk cooperate to trigger actin polymerization during Shigella invasion of epithelial cells. J. Cell Biol. 166 (2004) 225-235
    • (2004) J. Cell Biol. , vol.166 , pp. 225-235
    • Bougneres, L.1
  • 29
    • 0034769365 scopus 로고    scopus 로고
    • Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
    • Lommel S., et al. Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2 (2001) 850-857
    • (2001) EMBO Rep. , vol.2 , pp. 850-857
    • Lommel, S.1
  • 30
    • 30344475861 scopus 로고    scopus 로고
    • Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions
    • Coyne C.B., and Bergelson J.M. Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell 124 (2006) 119-131
    • (2006) Cell , vol.124 , pp. 119-131
    • Coyne, C.B.1    Bergelson, J.M.2
  • 31
    • 0030932978 scopus 로고    scopus 로고
    • The murine AIDS virus Gag precursor protein binds to the SH3 domain of c-Abl
    • Dupraz P., et al. The murine AIDS virus Gag precursor protein binds to the SH3 domain of c-Abl. J. Virol. 71 (1997) 2615-2620
    • (1997) J. Virol. , vol.71 , pp. 2615-2620
    • Dupraz, P.1
  • 32
    • 24944519321 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated bacterial effector proteins: the enemies within
    • Backert S., and Selbach M. Tyrosine-phosphorylated bacterial effector proteins: the enemies within. Trends Microbiol. 13 (2005) 476-484
    • (2005) Trends Microbiol. , vol.13 , pp. 476-484
    • Backert, S.1    Selbach, M.2
  • 33
    • 0028938721 scopus 로고
    • Catalytic specificity of protein-tyrosine kinases is critical for selective signalling
    • Songyang Z., et al. Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature 373 (1995) 536-539
    • (1995) Nature , vol.373 , pp. 536-539
    • Songyang, Z.1
  • 34
    • 0037197805 scopus 로고    scopus 로고
    • Grb2 and Nck act cooperatively to promote actin-based motility of vaccinia virus
    • Scaplehorn N., et al. Grb2 and Nck act cooperatively to promote actin-based motility of vaccinia virus. Curr. Biol. 12 (2002) 740-745
    • (2002) Curr. Biol. , vol.12 , pp. 740-745
    • Scaplehorn, N.1
  • 35
    • 22544470270 scopus 로고    scopus 로고
    • Disabling poxvirus pathogenesis by inhibition of Abl-family tyrosine kinases
    • Reeves P.M., et al. Disabling poxvirus pathogenesis by inhibition of Abl-family tyrosine kinases. Nat. Med. 11 (2005) 731-739
    • (2005) Nat. Med. , vol.11 , pp. 731-739
    • Reeves, P.M.1
  • 36
    • 32944461681 scopus 로고    scopus 로고
    • Abl collaborates with Src family kinases to stimulate actin-based motility of vaccinia virus
    • Newsome T.P., et al. Abl collaborates with Src family kinases to stimulate actin-based motility of vaccinia virus. Cell. Microbiol. 8 (2006) 233-241
    • (2006) Cell. Microbiol. , vol.8 , pp. 233-241
    • Newsome, T.P.1
  • 37
    • 0037330293 scopus 로고    scopus 로고
    • Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7
    • Campellone K.G., and Leong J.M. Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7. Curr. Opin. Microbiol. 6 (2003) 82-90
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 82-90
    • Campellone, K.G.1    Leong, J.M.2
  • 38
    • 31844451228 scopus 로고    scopus 로고
    • Subversion of actin dynamics by EPEC and EHEC
    • Caron E., et al. Subversion of actin dynamics by EPEC and EHEC. Curr. Opin. Microbiol. 9 (2006) 40-45
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 40-45
    • Caron, E.1
  • 39
    • 13444252561 scopus 로고    scopus 로고
    • EPEC's weapons of mass subversion
    • Dean P., et al. EPEC's weapons of mass subversion. Curr. Opin. Microbiol. 8 (2005) 28-34
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 28-34
    • Dean, P.1
  • 40
    • 17144405654 scopus 로고    scopus 로고
    • Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir
    • Campellone K.G., and Leong J.M. Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir. Mol. Microbiol. 56 (2005) 416-432
    • (2005) Mol. Microbiol. , vol.56 , pp. 416-432
    • Campellone, K.G.1    Leong, J.M.2
  • 41
    • 33947210792 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli Tir is an SH2/3 ligand that recruits and activates tyrosine kinases required for pedestal formation
    • Bommarius B., et al. Enteropathogenic Escherichia coli Tir is an SH2/3 ligand that recruits and activates tyrosine kinases required for pedestal formation. Mol. Microbiol. 63 (2007) 1748-1768
    • (2007) Mol. Microbiol. , vol.63 , pp. 1748-1768
    • Bommarius, B.1
  • 42
    • 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. Nat. Cell Biol. 1 (1999) 389-391
    • (1999) Nat. Cell Biol. , vol.1 , pp. 389-391
    • Kalman, D.1
  • 43
    • 0034842129 scopus 로고    scopus 로고
    • Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells
    • Gruenheid S., et al. Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells. Nat. Cell Biol. 3 (2001) 856-859
    • (2001) Nat. Cell Biol. , vol.3 , pp. 856-859
    • Gruenheid, S.1
  • 44
    • 3343010235 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli use redundant tyrosine kinases to form actin pedestals
    • Swimm A., et al. Enteropathogenic Escherichia coli use redundant tyrosine kinases to form actin pedestals. Mol. Biol. Cell 15 (2004) 3520-3529
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3520-3529
    • Swimm, A.1
  • 45
    • 0034659385 scopus 로고    scopus 로고
    • Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with alpha-actinin
    • Goosney D.L., et al. Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with alpha-actinin. Curr. Biol. 10 (2000) 735-738
    • (2000) Curr. Biol. , vol.10 , pp. 735-738
    • Goosney, D.L.1
  • 46
    • 0035997135 scopus 로고    scopus 로고
    • Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC)
    • Huang L., et al. Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC). Cell Motil. Cytoskeleton 52 (2002) 255-265
    • (2002) Cell Motil. Cytoskeleton , vol.52 , pp. 255-265
    • Huang, L.1
  • 47
    • 31844453155 scopus 로고    scopus 로고
    • Host protein interactions with enteropathogenic Escherichia coli (EPEC): 14-3-3tau binds Tir and has a role in EPEC-induced actin polymerization
    • Patel A., et al. Host protein interactions with enteropathogenic Escherichia coli (EPEC): 14-3-3tau binds Tir and has a role in EPEC-induced actin polymerization. Cell. Microbiol. 8 (2006) 55-71
    • (2006) Cell. Microbiol. , vol.8 , pp. 55-71
    • Patel, A.1
  • 48
    • 0037386567 scopus 로고    scopus 로고
    • Citrobacter rodentium translocated intimin receptor (Tir) is an essential virulence factor needed for actin condensation, intestinal colonization and colonic hyperplasia in mice
    • Deng W., et al. Citrobacter rodentium translocated intimin receptor (Tir) is an essential virulence factor needed for actin condensation, intestinal colonization and colonic hyperplasia in mice. Mol. Microbiol. 48 (2003) 95-115
    • (2003) Mol. Microbiol. , vol.48 , pp. 95-115
    • Deng, W.1
  • 49
    • 0036227053 scopus 로고    scopus 로고
    • c-Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs
    • Stein M., et al. c-Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs. Mol. Microbiol. 43 (2002) 971-980
    • (2002) Mol. Microbiol. , vol.43 , pp. 971-980
    • Stein, M.1
  • 50
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • Backert S., and Meyer T.F. Type IV secretion systems and their effectors in bacterial pathogenesis. Curr. Opin. Microbiol. 9 (2006) 207-217
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 51
    • 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 (2002) 6775-6778
    • (2002) J. Biol. Chem. , vol.277 , pp. 6775-6778
    • Selbach, M.1
  • 52
    • 0037423309 scopus 로고    scopus 로고
    • Attenuation of Helicobacter pylori CagA x SHP-2 signalling by interaction between CagA and C-terminal Src kinase
    • Tsutsumi R., et al. Attenuation of Helicobacter pylori CagA x SHP-2 signalling by interaction between CagA and C-terminal Src kinase. J. Biol. Chem. 278 (2003) 3664-3670
    • (2003) J. Biol. Chem. , vol.278 , pp. 3664-3670
    • Tsutsumi, R.1
  • 53
    • 0037415684 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation
    • Selbach M., et al. The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation. EMBO J. 22 (2003) 515-528
    • (2003) EMBO J. , vol.22 , pp. 515-528
    • Selbach, M.1
  • 54
    • 5644225534 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein induces tyrosine dephosphorylation of ezrin
    • Selbach M., et al. The Helicobacter pylori CagA protein induces tyrosine dephosphorylation of ezrin. Proteomics 4 (2004) 2961-2968
    • (2004) Proteomics , vol.4 , pp. 2961-2968
    • Selbach, M.1
  • 55
    • 34047245107 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin
    • Moese S., et al. The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin. Cell. Microbiol. 9 (2007) 1148-1161
    • (2007) Cell. Microbiol. , vol.9 , pp. 1148-1161
    • Moese, S.1
  • 56
    • 34249308195 scopus 로고    scopus 로고
    • Phosphorylation of Helicobacter pylori CagA by c-Abl leads to cell motility
    • Poppe M., et al. Phosphorylation of Helicobacter pylori CagA by c-Abl leads to cell motility. Oncogene 26 (2007) 3462-3472
    • (2007) Oncogene , vol.26 , pp. 3462-3472
    • Poppe, M.1
  • 57
    • 34247255905 scopus 로고    scopus 로고
    • Activation of Abl by Helicobacter pylori: a novel kinase for CagA and crucial mediator of host cell scattering
    • Tammer I., et al. Activation of Abl by Helicobacter pylori: a novel kinase for CagA and crucial mediator of host cell scattering. Gastroenterol. 132 (2007) 1309-1319
    • (2007) Gastroenterol. , vol.132 , pp. 1309-1319
    • Tammer, I.1
  • 58
    • 35349031591 scopus 로고    scopus 로고
    • Helicobacter exploits integrin for type IV secretion and kinase activation
    • Kwok T., et al. Helicobacter exploits integrin for type IV secretion and kinase activation. Nature 449 (2007) 862-866
    • (2007) Nature , vol.449 , pp. 862-866
    • Kwok, T.1
  • 59
    • 27744471043 scopus 로고    scopus 로고
    • Interaction of CagA with Crk plays an important role in Helicobacter pylori-induced loss of gastric epithelial cell adhesion
    • Suzuki M., et al. Interaction of CagA with Crk plays an important role in Helicobacter pylori-induced loss of gastric epithelial cell adhesion. J. Exp. Med. 202 (2005) 1235-1247
    • (2005) J. Exp. Med. , vol.202 , pp. 1235-1247
    • Suzuki, M.1
  • 60
    • 34250370846 scopus 로고    scopus 로고
    • Use of a novel coinfection system reveals a role for Rac1, H-Ras, and CrkII phosphorylation in Helicobacter pylori-induced host cell actin cytoskeletal rearrangements
    • Brandt S., et al. Use of a novel coinfection system reveals a role for Rac1, H-Ras, and CrkII phosphorylation in Helicobacter pylori-induced host cell actin cytoskeletal rearrangements. FEMS Immunol. Med. Microbiol. 50 (2007) 190-205
    • (2007) FEMS Immunol. Med. Microbiol. , vol.50 , pp. 190-205
    • Brandt, S.1
  • 61
    • 0036512370 scopus 로고    scopus 로고
    • B-Raf/Rap1 signalling, but not c-Raf-1/Ras, induces the histidine decarboxylase promoter in Helicobacter pylori infection
    • Wessler S., et al. B-Raf/Rap1 signalling, but not c-Raf-1/Ras, induces the histidine decarboxylase promoter in Helicobacter pylori infection. FASEB J. 16 (2002) 417-419
    • (2002) FASEB J. , vol.16 , pp. 417-419
    • Wessler, S.1
  • 62
    • 33847733565 scopus 로고    scopus 로고
    • Helicobacter pylori CagA induces AGS cell elongation through a cell retraction defect that is independent of Cdc42, Rac1, and Arp2/3
    • Bourzac K.M., et al. Helicobacter pylori CagA induces AGS cell elongation through a cell retraction defect that is independent of Cdc42, Rac1, and Arp2/3. Infect. Immun. 75 (2007) 1203-1213
    • (2007) Infect. Immun. , vol.75 , pp. 1203-1213
    • Bourzac, K.M.1
  • 63
    • 33645214468 scopus 로고    scopus 로고
    • Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA
    • Tsutsumi R., et al. Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA. Mol. Cell. Biol. 26 (2006) 261-276
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 261-276
    • Tsutsumi, R.1
  • 64
    • 23044463653 scopus 로고    scopus 로고
    • Activation of beta-catenin by carcinogenic Helicobacter pylori
    • Franco A.T., et al. Activation of beta-catenin by carcinogenic Helicobacter pylori. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 10646-10651
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 10646-10651
    • Franco, A.T.1
  • 65
    • 34447519946 scopus 로고    scopus 로고
    • Helicobacter pylori CagA interacts with E-cadherin and deregulates the beta-catenin signal that promotes intestinal transdifferentiation in gastric epithelial cells
    • Murata-Kamiya N., et al. Helicobacter pylori CagA interacts with E-cadherin and deregulates the beta-catenin signal that promotes intestinal transdifferentiation in gastric epithelial cells. Oncogene 26 (2007) 4617-4626
    • (2007) Oncogene , vol.26 , pp. 4617-4626
    • Murata-Kamiya, N.1
  • 66
    • 34548621770 scopus 로고    scopus 로고
    • CagA-independent disruption of adherence junction complexes involves E-cadherin shedding and implies multiple steps in Helicobacter pylori pathogenicity
    • Weydig C., et al. CagA-independent disruption of adherence junction complexes involves E-cadherin shedding and implies multiple steps in Helicobacter pylori pathogenicity. Exp. Cell Res. 313 (2007) 3459-3471
    • (2007) Exp. Cell Res. , vol.313 , pp. 3459-3471
    • Weydig, C.1
  • 67
    • 0036809776 scopus 로고    scopus 로고
    • Grb2 is a key mediator of Helicobacter pylori CagA protein activities
    • Mimuro H., et al. Grb2 is a key mediator of Helicobacter pylori CagA protein activities. Mol. Cell 10 (2002) 745-755
    • (2002) Mol. Cell , vol.10 , pp. 745-755
    • Mimuro, H.1
  • 68
    • 21544441173 scopus 로고    scopus 로고
    • NF-κB activation and potentiation of proinflammatory responses by the Helicobacter pylori CagA protein
    • Brandt S., et al. NF-κB activation and potentiation of proinflammatory responses by the Helicobacter pylori CagA protein. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 9300-9305
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9300-9305
    • Brandt, S.1
  • 69
    • 34249090814 scopus 로고    scopus 로고
    • Helicobacter pylori CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity
    • Saadat I., et al. Helicobacter pylori CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity. Nature 447 (2007) 330-333
    • (2007) Nature , vol.447 , pp. 330-333
    • Saadat, I.1
  • 70
    • 4143085008 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins
    • Park J., et al. Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins. Cell. Microbiol. 6 (2004) 743-751
    • (2004) Cell. Microbiol. , vol.6 , pp. 743-751
    • Park, J.1
  • 71
    • 34147154867 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection
    • Ijdo J.W., et al. Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection. Cell. Microbiol. 9 (2007) 1284-1296
    • (2007) Cell. Microbiol. , vol.9 , pp. 1284-1296
    • Ijdo, J.W.1
  • 72
    • 34848862803 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection
    • Lin M., et al. Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection. Cell. Microbiol. 9 (2007) 2644-2657
    • (2007) Cell. Microbiol. , vol.9 , pp. 2644-2657
    • Lin, M.1
  • 73
    • 4544235743 scopus 로고    scopus 로고
    • c-Src and cooperating partners in human cancer
    • Ishizawar R., and Parsons S.J. c-Src and cooperating partners in human cancer. Cancer Cell 6 (2004) 209-214
    • (2004) Cancer Cell , vol.6 , pp. 209-214
    • Ishizawar, R.1    Parsons, S.J.2
  • 74
    • 37049014938 scopus 로고    scopus 로고
    • Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib reveal novel kinase and non-kinase targets
    • Rix U., et al. Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib reveal novel kinase and non-kinase targets. Blood 110 (2007) 4055-4063
    • (2007) Blood , vol.110 , pp. 4055-4063
    • Rix, U.1
  • 75
    • 34247470836 scopus 로고    scopus 로고
    • Second generation inhibitors of BCR-ABL for the treatment of imatinib-resistant chronic myeloid leukaemia
    • Weisberg E., et al. Second generation inhibitors of BCR-ABL for the treatment of imatinib-resistant chronic myeloid leukaemia. Nat. Rev. Cancer 7 (2007) 345-356
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 345-356
    • Weisberg, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.