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Volumn 9, Issue , 2011, Pages

Regulation of the actin cytoskeleton in Helicobacter pylori-induced migration and invasive growth of gastric epithelial cells

Author keywords

actin cytoskeleton; CagA; Helicobacter pylori; type IV secretion system

Indexed keywords

ACTIN; ADAPTOR PROTEIN; CAGA PROTEIN; F ACTIN; G ACTIN; GUANOSINE TRIPHOSPHATASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84865972972     PISSN: None     EISSN: 1478811X     Source Type: Journal    
DOI: 10.1186/1478-811X-9-27     Document Type: Review
Times cited : (20)

References (86)
  • 1
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • DOI 10.1152/physrev.00021.2007
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration. C Le Clainche, MF Carlier, Physiol Rev 2008 88 489 513 10.1152/physrev.00021.2007 18391171 (Pubitemid 351520086)
    • (2008) Physiological Reviews , vol.88 , Issue.2 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.-F.2
  • 2
    • 0036498546 scopus 로고    scopus 로고
    • The lamellipodium: Where motility begins
    • DOI 10.1016/S0962-8924(01)02237-1, PII S0962892401022371
    • The lamellipodium: where motility begins. JV Small, T Stradal, E Vignal, K Rottner, Trends Cell Biol 2002 12 112 120 10.1016/S0962-8924(01)02237-1 11859023 (Pubitemid 34164650)
    • (2002) Trends in Cell Biology , vol.12 , Issue.3 , pp. 112-120
    • Small J.Victor1    Stradal, T.2    Vignal, E.3    Rottner, K.4
  • 3
    • 30844472903 scopus 로고    scopus 로고
    • The making of filopodia
    • DOI 10.1016/j.ceb.2005.11.002, PII S095506740500178X, Cell Structure and Dynamics
    • The making of filopodia. J Faix, K Rottner, Curr Opin Cell Biol 2006 18 18 25 10.1016/j.ceb.2005.11.002 16337369 (Pubitemid 43107603)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.1 , pp. 18-25
    • Faix, J.1    Rottner, K.2
  • 4
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • DOI 10.1016/j.tcb.2006.08.006, PII S0962892406002236, Membrane Dynamics
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. AJ Ridley, Trends Cell Biol 2006 16 522 529 10.1016/j.tcb.2006.08. 006 16949823 (Pubitemid 44444995)
    • (2006) Trends in Cell Biology , vol.16 , Issue.10 , pp. 522-529
    • Ridley, A.J.1
  • 5
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • 10.1038/nrm2957 20729930
    • Cell adhesion: integrating cytoskeletal dynamics and cellular tension. JT Parsons, AR Horwitz, MA Schwartz, Nat Rev Mol Cell Biol 2010 11 633 643 10.1038/nrm2957 20729930
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 6
    • 70349332774 scopus 로고    scopus 로고
    • Focal adhesion kinase: Switching between GAPs and GEFs in the regulation of cell motility
    • 10.1016/j.ceb.2009.05.006 19525103
    • Focal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility. A Tomar, DD Schlaepfer, Curr Opin Cell Biol 2009 21 676 683 10.1016/j.ceb.2009.05.006 19525103
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 676-683
    • Tomar, A.1    Schlaepfer, D.D.2
  • 7
    • 0034715895 scopus 로고    scopus 로고
    • Rho GTPases: Signaling, migration, and invasion
    • 10.1006/excr.2000.5049 11082269
    • Rho GTPases: signaling, migration, and invasion. AA Schmitz, EE Govek, B Bottner, L Van Aelst, Exp Cell Res 2000 261 1 12 10.1006/excr.2000.5049 11082269
    • (2000) Exp Cell Res , vol.261 , pp. 1-12
    • Schmitz, A.A.1    Govek, E.E.2    Bottner, B.3    Van Aelst, L.4
  • 8
    • 0030911424 scopus 로고    scopus 로고
    • P140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • DOI 10.1093/emboj/16.11.3044
    • p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. N Watanabe, P Madaule, T Reid, T Ishizaki, G Watanabe, A Kakizuka, Y Saito, K Nakao, BM Jockusch, S Narumiya, EMBO J 1997 16 3044 3056 10.1093/emboj/16.11.3044 9214622 (Pubitemid 27234944)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3044-3056
    • Watanabe, N.1    Madaule, P.2    Reid, T.3    Ishizaki, T.4    Watanabe, G.5    Kakizuka, A.6    Saito, Y.7    Nakao, K.8    Jockusch, B.M.9    Narumiya, S.10
  • 9
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts
    • DOI 10.1083/jcb.150.4.797
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. G Totsukawa, Y Yamakita, S Yamashiro, DJ Hartshorne, Y Sasaki, F Matsumura, J Cell Biol 2000 150 797 806 10.1083/jcb.150.4.797 10953004 (Pubitemid 30663416)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6
  • 10
    • 78049354889 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric cancer: Factors that modulate disease risk
    • 10.1128/CMR.00011-10 20930071
    • Helicobacter pylori and gastric cancer: factors that modulate disease risk. LE Wroblewski, RM Peek Jr, KT Wilson, Clin Microbiol Rev 2010 23 713 739 10.1128/CMR.00011-10 20930071
    • (2010) Clin Microbiol Rev , vol.23 , pp. 713-739
    • Wroblewski, L.E.1    Peek Jr., J.R.M.2    Wilson, K.T.3
  • 11
    • 80052626348 scopus 로고    scopus 로고
    • Genetic predisposition to Helicobacter pylori-induced gastric precancerous conditions
    • 10.4251/wjgo.v2.i10.369 21160888
    • Genetic predisposition to Helicobacter pylori-induced gastric precancerous conditions. A Hishida, K Matsuo, Y Goto, N Hamajima, World J Gastrointest Oncol 2010 2 369 379 10.4251/wjgo.v2.i10.369 21160888
    • (2010) World J Gastrointest Oncol , vol.2 , pp. 369-379
    • Hishida, A.1    Matsuo, K.2    Goto, Y.3    Hamajima, N.4
  • 12
    • 77952534868 scopus 로고    scopus 로고
    • H. pylori-Eradication Therapy Increases RUNX3 Expression in the Glandular Epithelial Cells in Enlarged-Fold Gastritis
    • 10.3164/jcbn.09-127 20490322
    • H. pylori-Eradication Therapy Increases RUNX3 Expression in the Glandular Epithelial Cells in Enlarged-Fold Gastritis. M Suzuki, H Suzuki, Y Minegishi, K Ito, T Nishizawa, T Hibi, J Clin Biochem Nutr 2010 46 259 264 10.3164/jcbn.09-127 20490322
    • (2010) J Clin Biochem Nutr , vol.46 , pp. 259-264
    • Suzuki, M.1    Suzuki, H.2    Minegishi, Y.3    Ito, K.4    Nishizawa, T.5    Hibi, T.6
  • 14
    • 0028694306 scopus 로고
    • Schistosomes, liver flukes and Helicobacter pylori. IARC Working Group on the Evaluation of Carcinogenic Risks to Humans. Lyon, 7-14 June 1994
    • 7715068
    • Schistosomes, liver flukes and Helicobacter pylori. IARC Working Group on the Evaluation of Carcinogenic Risks to Humans. Lyon, 7-14 June 1994. IARC Monogr Eval Carcinog Risks Hum 1994 61 1 241 7715068
    • (1994) IARC Monogr Eval Carcinog Risks Hum , vol.61 , pp. 1-241
  • 15
    • 79959461087 scopus 로고    scopus 로고
    • Complex Cellular Responses of Helicobacter pylori-Colonized Gastric Adenocarcinoma Cells
    • 10.1128/IAI.01350-10 21402757
    • Complex Cellular Responses of Helicobacter pylori-Colonized Gastric Adenocarcinoma Cells. S Schneider, G Carra, U Sahin, B Hoy, G Rieder, S Wessler, Infect Immun 2011 79 2362 2371 10.1128/IAI.01350-10 21402757
    • (2011) Infect Immun , vol.79 , pp. 2362-2371
    • Schneider, S.1    Carra, G.2    Sahin, U.3    Hoy, B.4    Rieder, G.5    Wessler, S.6
  • 16
    • 23344452849 scopus 로고    scopus 로고
    • Analysis of cell type-specific responses mediated by the type IV secretion system of Helicobacter pylori
    • DOI 10.1128/IAI.73.8.4643-4652.2005
    • Analysis of cell type-specific responses mediated by the type IV secretion system of Helicobacter pylori. B Bauer, S Moese, S Bartfeld, TF Meyer, M Selbach, Infect Immun 2005 73 4643 4652 10.1128/IAI.73.8.4643-4652.2005 16040977 (Pubitemid 41105620)
    • (2005) Infection and Immunity , vol.73 , Issue.8 , pp. 4643-4652
    • Bauer, B.1    Moese, S.2    Bartfeld, S.3    Meyer, T.F.4    Selbach, M.5
  • 17
    • 69449084254 scopus 로고    scopus 로고
    • Pathogenesis of Helicobacter pylori infection
    • 19712163
    • Pathogenesis of Helicobacter pylori infection. AC Costa, C Figueiredo, E Touati, Helicobacter 2009 14 Suppl 1 15 20 19712163
    • (2009) Helicobacter , vol.14 , Issue.SUPPL. 1 , pp. 15-20
    • Costa, A.C.1    Figueiredo, C.2    Touati, E.3
  • 18
    • 0042932364 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation
    • DOI 10.1126/science.1086871
    • Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation. B Gebert, W Fischer, E Weiss, R Hoffmann, R Haas, Science 2003 301 1099 1102 10.1126/science.1086871 12934009 (Pubitemid 37022312)
    • (2003) Science , vol.301 , Issue.5636 , pp. 1099-1102
    • Gebert, B.1    Fischer, W.2    Weiss, E.3    Hoffmann, R.4    Haas, R.5
  • 22
    • 79953701623 scopus 로고    scopus 로고
    • Assembly and molecular mode of action of the Helicobacter pylori Cag type IV secretion apparatus
    • 10.1111/j.1742-4658.2011.08036.x 21352490
    • Assembly and molecular mode of action of the Helicobacter pylori Cag type IV secretion apparatus. W Fischer, FEBS J 2011 278 1203 1212 10.1111/j.1742-4658.2011.08036.x 21352490
    • (2011) FEBS J , vol.278 , pp. 1203-1212
    • Fischer, W.1
  • 23
    • 77952133535 scopus 로고    scopus 로고
    • The versatility of Helicobacter pylori CagA effector protein functions: The master key hypothesis
    • 10.1111/j.1523-5378.2010.00759.x 20557357
    • The versatility of Helicobacter pylori CagA effector protein functions: The master key hypothesis. S Backert, N Tegtmeyer, M Selbach, Helicobacter 2010 15 163 176 10.1111/j.1523-5378.2010.00759.x 20557357
    • (2010) Helicobacter , vol.15 , pp. 163-176
    • Backert, S.1    Tegtmeyer, N.2    Selbach, M.3
  • 27
    • 0029043658 scopus 로고
    • Infection with Helicobacter pylori strains possessing cagA is associated with an increased risk of developing adenocarcinoma of the stomach
    • 7743510
    • Infection with Helicobacter pylori strains possessing cagA is associated with an increased risk of developing adenocarcinoma of the stomach. MJ Blaser, GI Perez-Perez, H Kleanthous, TL Cover, RM Peek, PH Chyou, GN Stemmermann, A Nomura, Cancer Res 1995 55 2111 2115 7743510
    • (1995) Cancer Res , vol.55 , pp. 2111-2115
    • Blaser, M.J.1    Perez-Perez, G.I.2    Kleanthous, H.3    Cover, T.L.4    Peek, R.M.5    Chyou, P.H.6    Stemmermann, G.N.7    Nomura, A.8
  • 28
    • 0030975595 scopus 로고    scopus 로고
    • Risk for gastric cancer in people with CagA positive or CagA negative Helicobacter pylori infection
    • Risk for gastric cancer in people with CagA positive or CagA negative Helicobacter pylori infection. J Parsonnet, GD Friedman, N Orentreich, H Vogelman, Gut 1997 40 297 301 9135515 (Pubitemid 27145639)
    • (1997) Gut , vol.40 , Issue.3 , pp. 297-301
    • Parsonnet, J.1    Friedman, G.D.2    Orentreich, N.3    Vogelman, H.4
  • 29
    • 65049086892 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric carcinogenesis
    • 10.1007/s00535-009-0014-1 19271114
    • Helicobacter pylori and gastric carcinogenesis. M Hatakeyama, J Gastroenterol 2009 44 239 248 10.1007/s00535-009-0014-1 19271114
    • (2009) J Gastroenterol , vol.44 , pp. 239-248
    • Hatakeyama, M.1
  • 30
    • 19044366273 scopus 로고    scopus 로고
    • Helicobacter pylori cag-type IV secretion system facilitates corpus colonization to induce precancerous conditions in mongolian gerbils
    • DOI 10.1053/j.gastro.2005.02.064, PII S0016508505003963
    • Helicobacter pylori cag-type IV secretion system facilitates corpus colonization to induce precancerous conditions in Mongolian gerbils. G Rieder, JL Merchant, R Haas, Gastroenterology 2005 128 1229 1242 10.1053/j.gastro.2005. 02.064 15887107 (Pubitemid 40712175)
    • (2005) Gastroenterology , vol.128 , Issue.5 , pp. 1229-1242
    • Rieder, G.1    Merchant, J.L.2    Haas, R.3
  • 31
    • 62749161502 scopus 로고    scopus 로고
    • Helicobacter pylori cag-Pathogenicity island-dependent early immunological response triggers later precancerous gastric changes in Mongolian gerbils
    • 10.1371/journal.pone.0004754 19270747
    • Helicobacter pylori cag-Pathogenicity island-dependent early immunological response triggers later precancerous gastric changes in Mongolian gerbils. T Wiedemann, E Loell, S Mueller, M Stoeckelhuber, M Stolte, R Haas, G Rieder, PLoS One 2009 4 4754 10.1371/journal.pone.0004754 19270747
    • (2009) PLoS One , vol.4 , pp. 54754
    • Wiedemann, T.1    Loell, E.2    Mueller, S.3    Stoeckelhuber, M.4    Stolte, M.5    Haas, R.6    Rieder, G.7
  • 33
    • 48149105975 scopus 로고    scopus 로고
    • Molecular mechanisms of epithelial-barrier disruption by Helicobacter pylori
    • 10.1016/j.tim.2008.05.005 18619844
    • Molecular mechanisms of epithelial-barrier disruption by Helicobacter pylori. S Wessler, S Backert, Trends Microbiol 2008 16 397 405 10.1016/j.tim.2008.05.005 18619844
    • (2008) Trends Microbiol , vol.16 , pp. 397-405
    • Wessler, S.1    Backert, S.2
  • 34
    • 55649109075 scopus 로고    scopus 로고
    • Targeting focal adhesions:Helicobacter pylori-host communication in cell migration
    • 10.1186/1478-811X-6-2 18684322
    • Targeting focal adhesions:Helicobacter pylori-host communication in cell migration. S Schneider, C Weydig, S Wessler, Cell Commun Signal 2008 6 2 10.1186/1478-811X-6-2 18684322
    • (2008) Cell Commun Signal , vol.6 , pp. 2
    • Schneider, S.1    Weydig, C.2    Wessler, S.3
  • 35
    • 0034668172 scopus 로고    scopus 로고
    • Induction and regulation of epithelial-mesenchymal transitions
    • 10.1016/S0006-2952(00)00427-5 11007946
    • Induction and regulation of epithelial-mesenchymal transitions. B Boyer, AM Valles, N Edme, Biochem Pharmacol 2000 60 1091 1099 10.1016/S0006-2952(00) 00427-5 11007946
    • (2000) Biochem Pharmacol , vol.60 , pp. 1091-1099
    • Boyer, B.1    Valles, A.M.2    Edme, N.3
  • 36
    • 77954691423 scopus 로고    scopus 로고
    • Helicobacter pylori potentiates epithelial:mesenchymal transition in gastric cancer: Links to soluble HB-EGF, gastrin and matrix metalloproteinase-7
    • 10.1136/gut.2009.199794 20584780
    • Helicobacter pylori potentiates epithelial:mesenchymal transition in gastric cancer: links to soluble HB-EGF, gastrin and matrix metalloproteinase-7. Y Yin, AM Grabowska, PA Clarke, E Whelband, K Robinson, RH Argent, A Tobias, R Kumari, JC Atherton, SA Watson, Gut 2010 59 1037 1045 10.1136/gut.2009.199794 20584780
    • (2010) Gut , vol.59 , pp. 1037-1045
    • Yin, Y.1    Grabowska, A.M.2    Clarke, P.A.3    Whelband, E.4    Robinson, K.5    Argent, R.H.6    Tobias, A.7    Kumari, R.8    Atherton, J.C.9    Watson, S.A.10
  • 37
    • 77956459044 scopus 로고    scopus 로고
    • Rac and Rho GTPases in cancer cell motility control
    • 10.1186/1478-811X-8-23 20822528
    • Rac and Rho GTPases in cancer cell motility control. M Parri, P Chiarugi, Cell Commun Signal 2010 8 23 10.1186/1478-811X-8-23 20822528
    • (2010) Cell Commun Signal , vol.8 , pp. 23
    • Parri, M.1    Chiarugi, P.2
  • 39
    • 77955146804 scopus 로고    scopus 로고
    • Podosome-like structures of non-invasive carcinoma cells are replaced in epithelial-mesenchymal transition by actin comet-embedded invadopodia
    • 19656240
    • Podosome-like structures of non-invasive carcinoma cells are replaced in epithelial-mesenchymal transition by actin comet-embedded invadopodia. M Takkunen, M Hukkanen, M Liljestrom, R Grenman, I Virtanen, J Cell Mol Med 2010 14 1569 1593 19656240
    • (2010) J Cell Mol Med , vol.14 , pp. 1569-1593
    • Takkunen, M.1    Hukkanen, M.2    Liljestrom, M.3    Grenman, R.4    Virtanen, I.5
  • 42
    • 34548621770 scopus 로고    scopus 로고
    • CagA-independent disruption of adherence junction complexes involves E-cadherin shedding and implies multiple steps in Helicobacter pylori pathogenicity
    • DOI 10.1016/j.yexcr.2007.07.015, PII S0014482707003424
    • CagA-independent disruption of adherence junction complexes involves E-cadherin shedding and implies multiple steps in Helicobacter pylori pathogenicity. C Weydig, A Starzinski-Powitz, G Carra, J Lower, S Wessler, Exp Cell Res 2007 313 3459 3471 10.1016/j.yexcr.2007.07.015 17692843 (Pubitemid 47404551)
    • (2007) Experimental Cell Research , vol.313 , Issue.16 , pp. 3459-3471
    • Weydig, C.1    Starzinski-Powitz, A.2    Carra, G.3    Lower, J.4    Wessler, S.5
  • 43
    • 40549089536 scopus 로고    scopus 로고
    • Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation
    • DOI 10.1242/jcs.008037
    • Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation. I Ayala, M Baldassarre, G Giacchetti, G Caldieri, S Tete, A Luini, R Buccione, J Cell Sci 2008 121 369 378 10.1242/jcs.008037 18198194 (Pubitemid 351356708)
    • (2008) Journal of Cell Science , vol.121 , Issue.3 , pp. 369-378
    • Ayala, I.1    Baldassarre, M.2    Giacchetti, G.3    Caldieri, G.4    Tete, S.5    Luini, A.6    Buccione, R.7
  • 44
    • 0036809776 scopus 로고    scopus 로고
    • Grb2 is a key mediator of Helicobacter pylori CagA protein activities
    • DOI 10.1016/S1097-2765(02)00681-0
    • Grb2 is a key mediator of helicobacter pylori CagA protein activities. H Mimuro, T Suzuki, J Tanaka, M Asahi, R Haas, C Sasakawa, Mol Cell 2002 10 745 755 10.1016/S1097-2765(02)00681-0 12419219 (Pubitemid 35335631)
    • (2002) Molecular Cell , vol.10 , Issue.4 , pp. 745-755
    • Mimuro, H.1    Suzuki, T.2    Tanaka, J.3    Asahi, M.4    Haas, R.5    Sasakawa, C.6
  • 45
    • 78650043640 scopus 로고    scopus 로고
    • Abl kinases are required for invadopodia formation and chemokine-induced invasion
    • 10.1074/jbc.M110.147330 20937825
    • Abl kinases are required for invadopodia formation and chemokine-induced invasion. PS Smith-Pearson, EK Greuber, G Yogalingam, AM Pendergast, J Biol Chem 2010 285 40201 40211 10.1074/jbc.M110.147330 20937825
    • (2010) J Biol Chem , vol.285 , pp. 40201-40211
    • Smith-Pearson, P.S.1    Greuber, E.K.2    Yogalingam, G.3    Pendergast, A.M.4
  • 47
    • 33751539322 scopus 로고    scopus 로고
    • Podoplanin binds ERM proteins to activate RhoA and promote epithelial-mesenchymal transition
    • DOI 10.1242/jcs.03218
    • Podoplanin binds ERM proteins to activate RhoA and promote epithelial-mesenchymal transition. E Martin-Villar, D Megias, S Castel, MM Yurrita, S Vilaro, M Quintanilla, J Cell Sci 2006 119 4541 4553 10.1242/jcs.03218 17046996 (Pubitemid 44830653)
    • (2006) Journal of Cell Science , vol.119 , Issue.21 , pp. 4541-4553
    • Martin-Villar, E.1    Megias, D.2    Castel, S.3    Yurrita, M.M.4    Vilaro, S.5    Quintanilla, M.6
  • 48
    • 79955925370 scopus 로고    scopus 로고
    • The transmembrane domain of podoplanin is required for its association with lipid rafts and the induction of epithelial-mesenchymal transition
    • 10.1016/j.biocel.2011.02.010 21376833
    • The transmembrane domain of podoplanin is required for its association with lipid rafts and the induction of epithelial-mesenchymal transition. B Fernandez-Munoz, MM Yurrita, E Martin-Villar, P Carrasco-Ramirez, D Megias, J Renart, M Quintanilla, Int J Biochem Cell Biol 2011 43 886 896 10.1016/j.biocel.2011.02.010 21376833
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 886-896
    • Fernandez-Munoz, B.1    Yurrita, M.M.2    Martin-Villar, E.3    Carrasco-Ramirez, P.4    Megias, D.5    Renart, J.6    Quintanilla, M.7
  • 49
    • 5644225534 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein induces tyrosine dephosphorylation of ezrin
    • DOI 10.1002/pmic.200400915
    • The Helicobacter pylori CagA protein induces tyrosine dephosphorylation of ezrin. M Selbach, S Moese, S Backert, PR Jungblut, TF Meyer, Proteomics 2004 4 2961 2968 10.1002/pmic.200400915 15378755 (Pubitemid 39372379)
    • (2004) Proteomics , vol.4 , Issue.10 , pp. 2961-2968
    • Selbach, M.1    Moese, S.2    Backert, S.3    Jungblut, P.R.4    Meyer, T.F.5
  • 50
    • 79954572864 scopus 로고    scopus 로고
    • Knockdown of ezrin via RNA interference suppresses Helicobacter pylori-enhanced invasion of gastric cancer cells
    • 10.4161/cbt.11.8.14691 21282970
    • Knockdown of ezrin via RNA interference suppresses Helicobacter pylori-enhanced invasion of gastric cancer cells. LL Fan, DF Chen, CH Lan, KY Liu, DC Fang, Cancer Biol Ther 2011 11 746 752 10.4161/cbt.11.8.14691 21282970
    • (2011) Cancer Biol Ther , vol.11 , pp. 746-752
    • Fan, L.L.1    Chen, D.F.2    Lan, C.H.3    Liu, K.Y.4    Fang, D.C.5
  • 51
    • 2542635813 scopus 로고    scopus 로고
    • Helicobacter pylori induces AGS cell motility and elongation via independent signaling pathways
    • DOI 10.1128/IAI.72.6.3646-3649.2004
    • Helicobacter pylori induces AGS cell motility and elongation via independent signaling pathways. S Moese, M Selbach, T Kwok, V Brinkmann, W Konig, TF Meyer, S Backert, Infect Immun 2004 72 3646 3649 10.1128/IAI.72.6. 3646-3649.2004 15155677 (Pubitemid 38697796)
    • (2004) Infection and Immunity , vol.72 , Issue.6 , pp. 3646-3649
    • Moese, S.1    Selbach, M.2    Kwok, T.3    Brinkmann, V.4    Konig, W.5    Meyer, T.F.6    Backert, S.7
  • 52
    • 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
    • DOI 10.1128/IAI.01702-06
    • Helicobacter pylori CagA induces AGS cell elongation through a cell retraction defect that is independent of Cdc42, Rac1, and Arp2/3. KM Bourzac, CM Botham, K Guillemin, Infect Immun 2007 75 1203 1213 10.1128/IAI.01702-06 17194805 (Pubitemid 46385811)
    • (2007) Infection and Immunity , vol.75 , Issue.3 , pp. 1203-1213
    • Bourzac, K.M.1    Botham, C.M.2    Guillemin, K.3
  • 54
    • 0037415684 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation
    • DOI 10.1093/emboj/cdg050
    • The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation. M Selbach, S Moese, R Hurwitz, CR Hauck, TF Meyer, S Backert, EMBO J 2003 22 515 528 10.1093/emboj/cdg050 12554652 (Pubitemid 36193596)
    • (2003) EMBO Journal , vol.22 , Issue.3 , pp. 515-528
    • Selbach, M.1    Moese, S.2    Hurwitz, R.3    Hauck, C.R.4    Meyer, T.F.5    Backert, S.6
  • 56
    • 73349087208 scopus 로고    scopus 로고
    • Helicobacter pylori counteracts the apoptotic action of its VacA toxin by injecting the CagA protein into gastric epithelial cells
    • 10.1371/journal.ppat.1000603 19798427
    • Helicobacter pylori counteracts the apoptotic action of its VacA toxin by injecting the CagA protein into gastric epithelial cells. A Oldani, M Cormont, V Hofman, V Chiozzi, O Oregioni, A Canonici, A Sciullo, P Sommi, A Fabbri, V Ricci, P Boquet, PLoS Pathog 2009 5 1000603 10.1371/journal.ppat.1000603 19798427
    • (2009) PLoS Pathog , vol.5 , pp. 51000603
    • Oldani, A.1    Cormont, M.2    Hofman, V.3    Chiozzi, V.4    Oregioni, O.5    Canonici, A.6    Sciullo, A.7    Sommi, P.8    Fabbri, A.9    Ricci, V.10    Boquet, P.11
  • 57
    • 59849112591 scopus 로고    scopus 로고
    • Importance of EGF receptor, HER2/Neu and Erk1/2 kinase signalling for host cell elongation and scattering induced by the Helicobacter pylori CagA protein: Antagonistic effects of the vacuolating cytotoxin VacA
    • 10.1111/j.1462-5822.2008.01269.x 19046339
    • Importance of EGF receptor, HER2/Neu and Erk1/2 kinase signalling for host cell elongation and scattering induced by the Helicobacter pylori CagA protein: antagonistic effects of the vacuolating cytotoxin VacA. N Tegtmeyer, D Zabler, D Schmidt, R Hartig, S Brandt, S Backert, Cell Microbiol 2009 11 488 505 10.1111/j.1462-5822.2008.01269.x 19046339
    • (2009) Cell Microbiol , vol.11 , pp. 488-505
    • Tegtmeyer, N.1    Zabler, D.2    Schmidt, D.3    Hartig, R.4    Brandt, S.5    Backert, S.6
  • 58
    • 0037423309 scopus 로고    scopus 로고
    • Attenuation of Helicobacter pylori CagA·SHP-2 signaling by interaction between CagA and C-terminal Src kinase
    • DOI 10.1074/jbc.M208155200
    • Attenuation of Helicobacter pylori CagA × SHP-2 signaling by interaction between CagA and C-terminal Src kinase. R Tsutsumi, H Higashi, M Higuchi, M Okada, M Hatakeyama, J Biol Chem 2003 278 3664 3670 10.1074/jbc.M208155200 12446738 (Pubitemid 36801090)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 3664-3670
    • Tsutsumi, R.1    Higashi, H.2    Higuchi, M.3    Okada, M.4    Hatakeyama, M.5
  • 59
    • 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
    • DOI 10.1046/j.1365-2958.2001.02649.x
    • Phosphorylation of tyrosine 972 of the Helicobacter pylori CagA protein is essential for induction of a scattering phenotype in gastric epithelial cells. S Backert, S Moese, M Selbach, V Brinkmann, TF Meyer, Mol Microbiol 2001 42 631 644 11722731 (Pubitemid 33064475)
    • (2001) Molecular Microbiology , vol.42 , Issue.3 , pp. 631-644
    • Backert, S.1    Moese, S.2    Selbach, M.3    Brinkmann, V.4    Meyer, T.F.5
  • 60
    • 34249308195 scopus 로고    scopus 로고
    • Phosphorylation of Helicobacter pylori CagA by c-Abl leads to cell motility
    • DOI 10.1038/sj.onc.1210139, PII 1210139
    • Phosphorylation of Helicobacter pylori CagA by c-Abl leads to cell motility. M Poppe, SM Feller, G Romer, S Wessler, Oncogene 2007 26 3462 3472 10.1038/sj.onc.1210139 17160020 (Pubitemid 46816757)
    • (2007) Oncogene , vol.26 , Issue.24 , pp. 3462-3472
    • Poppe, M.1    Feller, S.M.2    Romer, G.3    Wessler, S.4
  • 61
    • 0037732638 scopus 로고    scopus 로고
    • Helicobacter pylori CagA protein targets the c-Met receptor and enhances the motogenic response
    • DOI 10.1083/jcb.200208039
    • Helicobacter pylori CagA protein targets the c-Met receptor and enhances the motogenic response. Y Churin, L Al-Ghoul, O Kepp, TF Meyer, W Birchmeier, M Naumann, J Cell Biol 2003 161 249 255 10.1083/jcb.200208039 12719469 (Pubitemid 36529844)
    • (2003) Journal of Cell Biology , vol.161 , Issue.2 , pp. 249-255
    • Churin, Y.1    Al-Ghoul, L.2    Kepp, O.3    Meyer, T.F.4    Birchmeier, W.5    Naumann, M.6
  • 62
    • 4544313059 scopus 로고    scopus 로고
    • Helicobacter pylori infection targets adherens junction regulatory proteins and results in increased rates of migration in human gastric epithelial cells
    • DOI 10.1128/IAI.72.9.5181-5192.2004
    • Helicobacter pylori infection targets adherens junction regulatory proteins and results in increased rates of migration in human gastric epithelial cells. VS Conlin, SB Curtis, Y Zhao, ED Moore, VC Smith, RM Meloche, BB Finlay, AM Buchan, Infect Immun 2004 72 5181 5192 10.1128/IAI.72.9.5181-5192.2004 15322013 (Pubitemid 39223404)
    • (2004) Infection and Immunity , vol.72 , Issue.9 , pp. 5181-5192
    • Conlin, V.S.1    Curtis, S.B.2    Zhao, Y.3    Moore, E.D.W.4    Smith, V.C.5    Meloche, R.M.6    Finlay, B.B.7    Buchan, A.M.J.8
  • 63
    • 34249802881 scopus 로고    scopus 로고
    • Helicobacter pylori alters the distribution of ZO-1 and p120ctn in primary human gastric epithelial cells
    • DOI 10.1016/j.prp.2007.04.003, PII S0344033807000854
    • Helicobacter pylori alters the distribution of ZO-1 and p120ctn in primary human gastric epithelial cells. S Krueger, T Hundertmark, D Kuester, T Kalinski, U Peitz, A Roessner, Pathol Res Pract 2007 203 433 444 10.1016/j.prp.2007.04.003 17509776 (Pubitemid 46852317)
    • (2007) Pathology Research and Practice , vol.203 , Issue.6 , pp. 433-444
    • Krueger, S.1    Hundertmark, T.2    Kuester, D.3    Kalinski, T.4    Peitz, U.5    Roessner, A.6
  • 65
    • 0035004343 scopus 로고    scopus 로고
    • Pathogenicity island-dependent activation of Rho GTPases Rac1 and Cdc42 in Helicobacter pylori infection
    • DOI 10.1046/j.1365-2958.2001.02443.x
    • Pathogenicity island-dependent activation of Rho GTPases Rac1 and Cdc42 in Helicobacter pylori infection. Y Churin, E Kardalinou, TF Meyer, M Naumann, Mol Microbiol 2001 40 815 823 10.1046/j.1365-2958.2001.02443.x 11401689 (Pubitemid 32523179)
    • (2001) Molecular Microbiology , vol.40 , Issue.4 , pp. 815-823
    • Churin, Y.1    Kardalinou, E.2    Meyer, T.F.3    Naumann, M.4
  • 66
    • 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
    • DOI 10.1111/j.1574-695X.2007.00234.x
    • 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. S Brandt, S Shafikhani, P Balachandran, S Jin, R Hartig, W Konig, J Engel, S Backert, FEMS Immunol Med Microbiol 2007 50 190 205 10.1111/j.1574-695X.2007.00234.x 17428306 (Pubitemid 46918646)
    • (2007) FEMS Immunology and Medical Microbiology , vol.50 , Issue.2 , pp. 190-205
    • Brandt, S.1    Shafikhani, S.2    Balachandran, P.3    Jin, S.4    Hartig, R.5    Konig, W.6    Engel, J.7    Backert, S.8
  • 67
    • 40749136361 scopus 로고    scopus 로고
    • OipA plays a role in Helicobacter pylori-induced focal adhesion kinase activation and cytoskeletal re-organization
    • DOI 10.1111/j.1462-5822.2007.01104.x
    • OipA plays a role in Helicobacter pylori-induced focal adhesion kinase activation and cytoskeletal re-organization. FH Tabassam, DY Graham, Y Yamaoka, Cell Microbiol 2008 10 1008 1020 10.1111/j.1462-5822.2007.01104.x 18067607 (Pubitemid 351386953)
    • (2008) Cellular Microbiology , vol.10 , Issue.4 , pp. 1008-1020
    • Tabassam, F.H.1    Graham, D.Y.2    Yamaoka, Y.3
  • 68
    • 46649109404 scopus 로고    scopus 로고
    • The beta1 integrin activates JNK independent of CagA, and JNK activation is required for Helicobacter pylori CagA+-induced motility of gastric cancer cells
    • 10.1074/jbc.M800289200 18356158
    • The beta1 integrin activates JNK independent of CagA, and JNK activation is required for Helicobacter pylori CagA+-induced motility of gastric cancer cells. JL Snider, C Allison, BH Bellaire, RL Ferrero, JA Cardelli, J Biol Chem 2008 283 13952 13963 10.1074/jbc.M800289200 18356158
    • (2008) J Biol Chem , vol.283 , pp. 13952-13963
    • Snider, J.L.1    Allison, C.2    Bellaire, B.H.3    Ferrero, R.L.4    Cardelli, J.A.5
  • 69
    • 0035890917 scopus 로고    scopus 로고
    • Multiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillin
    • DOI 10.1042/0264-6021:3600057
    • Multiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillin. MD Schaller, EM Schaefer, Biochem J 2001 360 57 66 10.1042/0264-6021:3600057 11695992 (Pubitemid 33081949)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 57-66
    • Schaller, M.D.1    Schaefer, E.M.2
  • 70
    • 27744471043 scopus 로고    scopus 로고
    • Interaction of CagA with Crk plays an important role in Helicobacter pylori-induced loss of gastric epithelial cell adhesion
    • DOI 10.1084/jem.20051027
    • Interaction of CagA with Crk plays an important role in Helicobacter pylori-induced loss of gastric epithelial cell adhesion. M Suzuki, H Mimuro, T Suzuki, M Park, T Yamamoto, C Sasakawa, J Exp Med 2005 202 1235 1247 10.1084/jem.20051027 16275761 (Pubitemid 41586954)
    • (2005) Journal of Experimental Medicine , vol.202 , Issue.9 , pp. 1235-1247
    • Suzuki, M.1    Mimuro, H.2    Suzuki, T.3    Park, M.4    Yamamoto, T.5    Sasakawa, C.6
  • 71
    • 79952825185 scopus 로고    scopus 로고
    • Helicobacter pylori CagA disrupts epithelial patterning by activating myosin light chain
    • 10.1371/journal.pone.0017856 21445303
    • Helicobacter pylori CagA disrupts epithelial patterning by activating myosin light chain. JB Muyskens, K Guillemin, PLoS One 2011 6 17856 10.1371/journal.pone.0017856 21445303
    • (2011) PLoS One , vol.6 , pp. 517856
    • Muyskens, J.B.1    Guillemin, K.2
  • 72
    • 54049093232 scopus 로고    scopus 로고
    • Differential phosphoproteome profiling reveals a functional role for VASP in Helicobacter pylori-induced cytoskeleton turnover in gastric epithelial cells
    • 10.1111/j.1462-5822.2008.01207.x 18637808
    • Differential phosphoproteome profiling reveals a functional role for VASP in Helicobacter pylori-induced cytoskeleton turnover in gastric epithelial cells. O Knauer, NA Binai, G Carra, T Beckhaus, KM Hanschmann, T Renne, S Backert, M Karas, S Wessler, Cell Microbiol 2008 10 2285 2296 10.1111/j.1462-5822.2008.01207.x 18637808
    • (2008) Cell Microbiol , vol.10 , pp. 2285-2296
    • Knauer, O.1    Binai, N.A.2    Carra, G.3    Beckhaus, T.4    Hanschmann, K.M.5    Renne, T.6    Backert, S.7    Karas, M.8    Wessler, S.9
  • 73
    • 0036510363 scopus 로고    scopus 로고
    • Src is the kinase of the Helicobacter pylori CagA protein in vitro and in vivo
    • DOI 10.1074/jbc.C100754200
    • Src is the kinase of the Helicobacter pylori CagA protein in vitro and in vivo. M Selbach, S Moese, CR Hauck, TF Meyer, S Backert, J Biol Chem 2002 277 6775 6778 10.1074/jbc.C100754200 11788577 (Pubitemid 34953058)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.9 , pp. 6775-6778
    • Selbach, M.1    Moese, S.2    Hauck, C.R.3    Meyer, T.F.4    Backert, S.5
  • 74
    • 0036227053 scopus 로고    scopus 로고
    • C-Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs
    • DOI 10.1046/j.1365-2958.2002.02781.x
    • c-Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs. M Stein, F Bagnoli, R Halenbeck, R Rappuoli, WJ Fantl, A Covacci, Mol Microbiol 2002 43 971 980 10.1046/j.1365-2958.2002.02781.x 11929545 (Pubitemid 34415720)
    • (2002) Molecular Microbiology , vol.43 , Issue.4 , pp. 971-980
    • Stein, M.1    Bagnoli, F.2    Halenbeck, R.3    Rappuoli, R.4    Fantl, W.J.5    Covacci, A.6
  • 75
    • 56749171378 scopus 로고    scopus 로고
    • Linking epithelial polarity and carcinogenesis by multitasking Helicobacter pylori virulence factor CagA
    • 10.1038/onc.2008.353 19029944
    • Linking epithelial polarity and carcinogenesis by multitasking Helicobacter pylori virulence factor CagA. M Hatakeyama, Oncogene 2008 27 7047 7054 10.1038/onc.2008.353 19029944
    • (2008) Oncogene , vol.27 , pp. 7047-7054
    • Hatakeyama, M.1
  • 76
    • 34247161416 scopus 로고    scopus 로고
    • CagA protein of Helicobacter pylori: A hijacker of gastric epithelial cell signaling
    • DOI 10.1016/j.bcp.2006.10.022, PII S0006295206006708
    • CagA protein of Helicobacter pylori: a hijacker of gastric epithelial cell signaling. O Handa, Y Naito, T Yoshikawa, Biochem Pharmacol 2007 73 1697 1702 10.1016/j.bcp.2006.10.022 17134680 (Pubitemid 46601402)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.11 , pp. 1697-1702
    • Handa, O.1    Naito, Y.2    Yoshikawa, T.3
  • 77
    • 34047245107 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin
    • DOI 10.1111/j.1462-5822.2006.00856.x
    • The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin. S Moese, M Selbach, V Brinkmann, A Karlas, B Haimovich, S Backert, TF Meyer, Cell Microbiol 2007 9 1148 1161 10.1111/j.1462-5822.2006.00856.x 17217431 (Pubitemid 46547135)
    • (2007) Cellular Microbiology , vol.9 , Issue.5 , pp. 1148-1161
    • Moese, S.1    Selbach, M.2    Brinkmann, V.3    Karlas, A.4    Haimovich, B.5    Backert, S.6    Meyer, T.F.7
  • 78
    • 0037169076 scopus 로고    scopus 로고
    • SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein
    • DOI 10.1126/science.1067147
    • SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein. H Higashi, R Tsutsumi, S Muto, T Sugiyama, T Azuma, M Asaka, M Hatakeyama, Science 2002 295 683 686 10.1126/science.1067147 11743164 (Pubitemid 34111828)
    • (2002) Science , vol.295 , Issue.5555 , pp. 683-686
    • Higashi, H.1    Tsutsumi, R.2    Muto, S.3    Sugiyama, T.4    Azuma, T.5    Asaka, M.6    Hatakeyama, M.7
  • 80
    • 0037439278 scopus 로고    scopus 로고
    • The CagA protein of Helicobacter pylori is translocated into epithelial cells and binds to SHP-2 in human gastric mucosa
    • DOI 10.1086/367807
    • The CagA protein of Helicobacter pylori is translocated into epithelial cells and binds to SHP-2 in human gastric mucosa. S Yamazaki, A Yamakawa, Y Ito, M Ohtani, H Higashi, M Hatakeyama, T Azuma, J Infect Dis 2003 187 334 337 10.1086/367807 12552462 (Pubitemid 36132651)
    • (2003) Journal of Infectious Diseases , vol.187 , Issue.2 , pp. 334-337
    • Yamazaki, S.1    Yamakawa, A.2    Ito, Y.3    Ohtani, M.4    Higashi, H.5    Hatakeyama, M.6    Azuma, T.7
  • 81
    • 33645214468 scopus 로고    scopus 로고
    • Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA
    • 10.1128/MCB.26.1.261-276.2006 16354697
    • Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA. R Tsutsumi, A Takahashi, T Azuma, H Higashi, M Hatakeyama, Mol Cell Biol 2006 26 261 276 10.1128/MCB.26.1.261-276. 2006 16354697
    • (2006) Mol Cell Biol , vol.26 , pp. 261-276
    • Tsutsumi, R.1    Takahashi, A.2    Azuma, T.3    Higashi, H.4    Hatakeyama, M.5
  • 82
    • 79958745867 scopus 로고    scopus 로고
    • Serine Phosphorylation of Cortactin Controls Focal Adhesion Kinase Activity and Cell Scattering Induced by Helicobacter pylori
    • 10.1016/j.chom.2011.05.007 21669400
    • Serine Phosphorylation of Cortactin Controls Focal Adhesion Kinase Activity and Cell Scattering Induced by Helicobacter pylori. N Tegtmeyer, R Wittelsberger, R Hartig, S Wessler, N Martinez-Quiles, S Backert, Cell Host Microbe 2011 9 520 531 10.1016/j.chom.2011.05.007 21669400
    • (2011) Cell Host Microbe , vol.9 , pp. 520-531
    • Tegtmeyer, N.1    Wittelsberger, R.2    Hartig, R.3    Wessler, S.4    Martinez-Quiles, N.5    Backert, S.6
  • 83
    • 0036512370 scopus 로고    scopus 로고
    • B-Raf/Rap1 signaling, but not c-Raf-1/Ras, induces the histidine decarboxylase promoter in Helicobacter pylori infection
    • 11790728
    • B-Raf/Rap1 signaling, but not c-Raf-1/Ras, induces the histidine decarboxylase promoter in Helicobacter pylori infection. S Wessler, UR Rapp, B Wiedenmann, TF Meyer, T Schoneberg, M Hocker, M Naumann, FASEB J 2002 16 417 419 11790728
    • (2002) FASEB J , vol.16 , pp. 417-419
    • Wessler, S.1    Rapp, U.R.2    Wiedenmann, B.3    Meyer, T.F.4    Schoneberg, T.5    Hocker, M.6    Naumann, M.7
  • 84
    • 70349433677 scopus 로고    scopus 로고
    • Helicobacter pylori activates protein kinase C delta to control Raf in MAP kinase signalling: Role in AGS epithelial cell scattering and elongation
    • 10.1002/cm.20373 19437514
    • Helicobacter pylori activates protein kinase C delta to control Raf in MAP kinase signalling: role in AGS epithelial cell scattering and elongation. S Brandt, S Wessler, R Hartig, S Backert, Cell Motil Cytoskeleton 2009 66 874 892 10.1002/cm.20373 19437514
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 874-892
    • Brandt, S.1    Wessler, S.2    Hartig, R.3    Backert, S.4
  • 85
    • 34247255905 scopus 로고    scopus 로고
    • Activation of Abl by Helicobacter pylori: A Novel Kinase for CagA and Crucial Mediator of Host Cell Scattering
    • DOI 10.1053/j.gastro.2007.01.050, PII S0016508507001898
    • Activation of Abl by Helicobacter pylori: a novel kinase for CagA and crucial mediator of host cell scattering. I Tammer, S Brandt, R Hartig, W Konig, S Backert, Gastroenterology 2007 132 1309 1319 10.1053/j.gastro.2007.01.050 17408661 (Pubitemid 46627580)
    • (2007) Gastroenterology , vol.132 , Issue.4 , pp. 1309-1319
    • Tammer, I.1    Brandt, S.2    Hartig, R.3    Konig, W.4    Backert, S.5
  • 86
    • 33846940534 scopus 로고    scopus 로고
    • East Asian-type Helicobacter pylori cytotoxin-associated gene A protein has a more significant effect on growth of rat gastric mucosal cells than the Western type
    • DOI 10.1111/j.1440-1746.2006.04531.x
    • East Asian-type Helicobacter pylori cytotoxin-associated gene A protein has a more significant effect on growth of rat gastric mucosal cells than the Western type. HY Fu, K Asahi, Y Hayashi, H Eguchi, H Murata, M Tsujii, S Tsuji, T Azuma, S Kawano, J Gastroenterol Hepatol 2007 22 355 362 10.1111/j.1440-1746. 2006.04531.x 17295767 (Pubitemid 46238765)
    • (2007) Journal of Gastroenterology and Hepatology , vol.22 , Issue.3 , pp. 355-362
    • Fu, H.Y.1    Asahi, K.2    Hayashi, Y.3    Eguchi, H.4    Murata, H.5    Tsujii, M.6    Tsuji, S.7    Azuma, T.8    Kawano, S.9


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