메뉴 건너뛰기




Volumn 8, Issue 5, 2016, Pages

New insights into VacA intoxication mediated through its cell surface receptors

Author keywords

Low density lipoprotein receptor related protein 1 (LRP1); Receptor like protein tyrosine phosphatase (RPTP) ; Receptors; RPTP ; Vacuolating cytotoxin (VacA)

Indexed keywords

CELL SURFACE RECEPTOR; FIBRONECTIN; LIPOPOLYSACCHARIDE; RECEPTOR LIKE PROTEIN TYROSINE PHOSPHATASE; VACUOLATING TOXIN; BACTERIAL PROTEIN; VACA PROTEIN, HELICOBACTER PYLORI;

EID: 84969135728     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins8050152     Document Type: Review
Times cited : (15)

References (100)
  • 1
    • 0035374653 scopus 로고    scopus 로고
    • Living dangerously: How Helicobacter pylori survives in the human stomach
    • [CrossRef] [PubMed]
    • Montecucco, C.; Rappuoli, R. Living dangerously: How Helicobacter pylori survives in the human stomach. Nat. Rev. Mol. Cell Biol. 2001, 2, 457-466. [CrossRef] [PubMed]
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 457-466
    • Montecucco, C.1    Rappuoli, R.2
  • 2
    • 42349107551 scopus 로고    scopus 로고
    • Association of inflammatory cytokine gene polymorphisms with platelet recovery in idiopathic thrombocytopenic purpura patients after the eradication of Helicobacter pylori
    • [CrossRef] [PubMed]
    • Suzuki, T.; Matsushima, M.; Shirakura, K.; Koike, J.; Masui, A.; Takagi, A.; Shirasugi, Y.; Ogawa, Y.; Shirai, T.; Mine, T. Association of inflammatory cytokine gene polymorphisms with platelet recovery in idiopathic thrombocytopenic purpura patients after the eradication of Helicobacter pylori. Digestion 2008, 77, 73-78. [CrossRef] [PubMed]
    • (2008) Digestion , vol.77 , pp. 73-78
    • Suzuki, T.1    Matsushima, M.2    Shirakura, K.3    Koike, J.4    Masui, A.5    Takagi, A.6    Shirasugi, Y.7    Ogawa, Y.8    Shirai, T.9    Mine, T.10
  • 3
    • 85047691456 scopus 로고    scopus 로고
    • Helicobacter pylori persistence: Biology and disease
    • [CrossRef] [PubMed]
    • Blaser, M.J.; Atherton, J.C. Helicobacter pylori persistence: Biology and disease. J. Clin. Investig. 2004, 113, 321-333. [CrossRef] [PubMed]
    • (2004) J. Clin. Investig. , vol.113 , pp. 321-333
    • Blaser, M.J.1    Atherton, J.C.2
  • 4
    • 33750075748 scopus 로고    scopus 로고
    • Helicobacter pylori persistence: An overview of interactions between H. pylori and host immune defenses
    • [CrossRef] [PubMed]
    • Algood, H.M.; Cover, T.L. Helicobacter pylori persistence: An overview of interactions between H. pylori and host immune defenses. Clin. Microbiol. Rev. 2006, 19, 597-613. [CrossRef] [PubMed]
    • (2006) Clin. Microbiol. Rev. , vol.19 , pp. 597-613
    • Algood, H.M.1    Cover, T.L.2
  • 5
    • 0037057683 scopus 로고    scopus 로고
    • Helicobacter pylori infection
    • [CrossRef] [PubMed]
    • Suerbaum, S.; Michetti, P. Helicobacter pylori infection. N. Engl. J. Med. 2002, 347, 1175-1186. [CrossRef] [PubMed]
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1175-1186
    • Suerbaum, S.1    Michetti, P.2
  • 8
    • 0035797916 scopus 로고    scopus 로고
    • Two distinctive cell binding patterns by vacuolating toxin fused with glutathione S-transferase: One high-affinity m1-specific binding and the other lower-affinity binding for variant m forms
    • [CrossRef] [PubMed]
    • Wang, W.C.; Wang, H.J.; Kuo, C.H. Two distinctive cell binding patterns by vacuolating toxin fused with glutathione S-transferase: One high-affinity m1-specific binding and the other lower-affinity binding for variant m forms. Biochemistry 2001, 40, 11887-11896. [CrossRef] [PubMed]
    • (2001) Biochemistry , vol.40 , pp. 11887-11896
    • Wang, W.C.1    Wang, H.J.2    Kuo, C.H.3
  • 9
    • 0031741917 scopus 로고    scopus 로고
    • Identification of the Helicobacter pylori VacA toxin domain active in the cell cytosol
    • [PubMed]
    • De Bernard, M.; Burroni, D.; Papini, E.; Rappuoli, R.; Telford, J.; Montecucco, C. Identification of the Helicobacter pylori VacA toxin domain active in the cell cytosol. Infect. Immun. 1998, 66, 6014-6016. [PubMed]
    • (1998) Infect. Immun. , vol.66 , pp. 6014-6016
    • De Bernard, M.1    Burroni, D.2    Papini, E.3    Rappuoli, R.4    Telford, J.5    Montecucco, C.6
  • 10
    • 0033515453 scopus 로고    scopus 로고
    • Identification of the minimal intracellular vacuolating domain of the Helicobacter pylori vacuolating toxin
    • [CrossRef] [PubMed]
    • Ye, D.; Willhite, D.C.; Blanke, S.R. Identification of the minimal intracellular vacuolating domain of the Helicobacter pylori vacuolating toxin. J. Biol. Chem. 1999, 274, 9277-9282. [CrossRef] [PubMed]
    • (1999) J. Biol. Chem. , vol.274 , pp. 9277-9282
    • Ye, D.1    Willhite, D.C.2    Blanke, S.R.3
  • 12
    • 29644446474 scopus 로고    scopus 로고
    • The cell-specific phenotype of the polymorphic VacA midregion is independent of the appearance of the cell surface receptor protein tyrosine phosphatase beta
    • [CrossRef] [PubMed]
    • Skibinski, D.A.; Genisset, C.; Barone, S.; Telford, J.L. The cell-specific phenotype of the polymorphic VacA midregion is independent of the appearance of the cell surface receptor protein tyrosine phosphatase beta. Infect. Immun. 2006, 74, 49-55. [CrossRef] [PubMed]
    • (2006) Infect. Immun. , vol.74 , pp. 49-55
    • Skibinski, D.A.1    Genisset, C.2    Barone, S.3    Telford, J.L.4
  • 14
    • 23844511511 scopus 로고    scopus 로고
    • Cytotoxicity and recognition of receptor-like protein tyrosine phosphatases, rptpalpha and rptpbeta, by Helicobacter pylori m2 VacA
    • [CrossRef] [PubMed]
    • De Guzman, B.B.; Hisatsune, J.; Nakayama, M.; Yahiro, K.;Wada, A.; Yamasaki, E.; Nishi, Y.; Yamazaki, S.; Azuma, T.; Ito, Y.; et al. Cytotoxicity and recognition of receptor-like protein tyrosine phosphatases, rptpalpha and rptpbeta, by Helicobacter pylori m2 VacA. Cell. Microbiol. 2005, 7, 1285-1293. [CrossRef] [PubMed]
    • (2005) Cell. Microbiol. , vol.7 , pp. 1285-1293
    • De Guzman, B.B.1    Hisatsune, J.2    Nakayama, M.3    Yahiro, K.4    Yamasaki, E.5    Nishi, Y.6    Yamazaki, S.7    Azuma, T.8    Ito, Y.9
  • 15
    • 0031845236 scopus 로고    scopus 로고
    • Vacuolating toxin production in clinical isolates of Helicobacter pylori with different VacA genotypes
    • [CrossRef] [PubMed]
    • Wang, H.J.; Kuo, C.H.; Yeh, A.A.; Chang, P.C.;Wang,W.C. Vacuolating toxin production in clinical isolates of Helicobacter pylori with different VacA genotypes. J. Infect. Dis. 1998, 178, 207-212. [CrossRef] [PubMed]
    • (1998) J. Infect. Dis. , vol.178 , pp. 207-212
    • Wang, H.J.1    Kuo, C.H.2    Yeh, A.A.3    Chang, P.C.4
  • 16
    • 0026739795 scopus 로고
    • Purification and characterization of the vacuolating toxin from Helicobacter pylori
    • [PubMed]
    • Cover, T.L.; Blaser, M.J. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J. Biol. Chem. 1992, 267, 10570-10575. [PubMed]
    • (1992) J. Biol. Chem. , vol.267 , pp. 10570-10575
    • Cover, T.L.1    Blaser, M.J.2
  • 17
    • 15944418287 scopus 로고    scopus 로고
    • Helicobacter pylori VacA, a paradigm for toxin multifunctionality
    • [CrossRef] [PubMed]
    • Cover, T.L.; Blanke, S.R. Helicobacter pylori VacA, a paradigm for toxin multifunctionality. Nat. Rev. Microbiol. 2005, 3, 320-332. [CrossRef] [PubMed]
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 320-332
    • Cover, T.L.1    Blanke, S.R.2
  • 18
    • 84874286760 scopus 로고    scopus 로고
    • Vacuolating cytotoxin A (VacA), a key toxin for Helicobacter pylori pathogenesis
    • [CrossRef] [PubMed]
    • Palframan, S.L.; Kwok, T.; Gabriel, K. Vacuolating cytotoxin A (VacA), a key toxin for Helicobacter pylori pathogenesis. Front. Cell. Infect. Microbiol. 2012, 2. [CrossRef] [PubMed]
    • (2012) Front. Cell. Infect. Microbiol. , pp. 2
    • Palframan, S.L.1    Kwok, T.2    Gabriel, K.3
  • 19
    • 84883761977 scopus 로고    scopus 로고
    • Pathogenesis of Helicobacter pylori infection
    • [CrossRef] [PubMed]
    • Cid, T.P.; Fernandez, M.C.; Benito Martinez, S.; Jones, N.L. Pathogenesis of Helicobacter pylori infection. Helicobacter 2013, 18 (Suppl. 1), 12-17. [CrossRef] [PubMed]
    • (2013) Helicobacter , vol.18 , pp. 12-17
    • Cid, T.P.1    Fernandez, M.C.2    Benito Martinez, S.3    Jones, N.L.4
  • 20
    • 84887022829 scopus 로고    scopus 로고
    • Modulation of autophagy by Helicobacter pylori and its role in gastric carcinogenesis
    • [CrossRef] [PubMed]
    • Greenfield, L.K.; Jones, N.L. Modulation of autophagy by Helicobacter pylori and its role in gastric carcinogenesis. Trends Microbiol. 2013, 21, 602-612. [CrossRef] [PubMed]
    • (2013) Trends Microbiol. , vol.21 , pp. 602-612
    • Greenfield, L.K.1    Jones, N.L.2
  • 21
    • 84859264679 scopus 로고    scopus 로고
    • Intoxication strategy of Helicobacter pylori VacA toxin
    • [CrossRef] [PubMed]
    • Boquet, P.; Ricci, V. Intoxication strategy of Helicobacter pylori VacA toxin. Trends Microbiol. 2012, 20, 165-174. [CrossRef] [PubMed]
    • (2012) Trends Microbiol. , vol.20 , pp. 165-174
    • Boquet, P.1    Ricci, V.2
  • 22
    • 84866339660 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating toxin A and apoptosis
    • [CrossRef] [PubMed]
    • Rassow, J. Helicobacter pylori vacuolating toxin A and apoptosis. Cell Commun. Signal. CCS 2011, 9. [CrossRef] [PubMed]
    • (2011) Cell Commun. Signal. CCS , pp. 9
    • Rassow, J.1
  • 23
    • 84874711674 scopus 로고    scopus 로고
    • Remodeling the host environment: Modulation of the gastric epithelium by the Helicobacter pylori vacuolating toxin (VacA)
    • [CrossRef] [PubMed]
    • Kim, I.J.; Blanke, S.R. Remodeling the host environment: Modulation of the gastric epithelium by the Helicobacter pylori vacuolating toxin (VacA). Front. Cell. Infect. Microbiol. 2012, 2. [CrossRef] [PubMed]
    • (2012) Front. Cell. Infect. Microbiol. , pp. 2
    • Kim, I.J.1    Blanke, S.R.2
  • 26
    • 0032981962 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating toxin forms anion-selective channels in planar lipid bilayers: Possible implications for the mechanism of cellular vacuolation
    • [CrossRef]
    • Tombola, F.; Carlesso, C.; Szabo, I.; de Bernard, M.; Reyrat, J.M.; Telford, J.L.; Rappuoli, R.; Montecucco, C.; Papini, E.; Zoratti, M. Helicobacter pylori vacuolating toxin forms anion-selective channels in planar lipid bilayers: Possible implications for the mechanism of cellular vacuolation. Biophys. J. 1999, 76, 1401-1409. [CrossRef]
    • (1999) Biophys. J. , vol.76 , pp. 1401-1409
    • Tombola, F.1    Carlesso, C.2    Szabo, I.3    De Bernard, M.4    Reyrat, J.M.5    Telford, J.L.6    Rappuoli, R.7    Montecucco, C.8    Papini, E.9    Zoratti, M.10
  • 27
    • 13044317274 scopus 로고    scopus 로고
    • Formation of anion-selective channels in the cell plasma membrane by the toxin VacA of Helicobacter pylori is required for its biological activity
    • [CrossRef] [PubMed]
    • Szabo, I.; Brutsche, S.; Tombola, F.; Moschioni, M.; Satin, B.; Telford, J.L.; Rappuoli, R.; Montecucco, C.; Papini, E.; Zoratti, M. Formation of anion-selective channels in the cell plasma membrane by the toxin VacA of Helicobacter pylori is required for its biological activity. EMBO J. 1999, 18, 5517-5527. [CrossRef] [PubMed]
    • (1999) EMBO J. , vol.18 , pp. 5517-5527
    • Szabo, I.1    Brutsche, S.2    Tombola, F.3    Moschioni, M.4    Satin, B.5    Telford, J.L.6    Rappuoli, R.7    Montecucco, C.8    Papini, E.9    Zoratti, M.10
  • 28
    • 84866130509 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein-1 (LRP1) mediates autophagy and apoptosis caused by Helicobacter pylori VacA
    • [CrossRef] [PubMed]
    • Yahiro, K.; Satoh, M.; Nakano, M.; Hisatsune, J.; Isomoto, H.; Sap, J.; Suzuki, H.; Nomura, F.; Noda, M.; Moss, J.; et al. Low-density lipoprotein receptor-related protein-1 (LRP1) mediates autophagy and apoptosis caused by Helicobacter pylori VacA. J. Biol. Chem. 2012, 287, 31104-31115. [CrossRef] [PubMed]
    • (2012) J. Biol. Chem. , vol.287 , pp. 31104-31115
    • Yahiro, K.1    Satoh, M.2    Nakano, M.3    Hisatsune, J.4    Isomoto, H.5    Sap, J.6    Suzuki, H.7    Nomura, F.8    Noda, M.9    Moss, J.10
  • 29
    • 0033579575 scopus 로고    scopus 로고
    • Activation of Helicobacter pylori VacA toxin by alkaline or acid conditions increases its binding to a 250-kDa receptor protein-tyrosine phosphatase beta
    • [CrossRef] [PubMed]
    • Yahiro, K.; Niidome, T.; Kimura, M.; Hatakeyama, T.; Aoyagi, H.; Kurazono, H.; Imagawa, K.; Wada, A.; Moss, J.; Hirayama, T. Activation of Helicobacter pylori VacA toxin by alkaline or acid conditions increases its binding to a 250-kDa receptor protein-tyrosine phosphatase beta. J. Biol. Chem. 1999, 274, 36693-36699. [CrossRef] [PubMed]
    • (1999) J. Biol. Chem. , vol.274 , pp. 36693-36699
    • Yahiro, K.1    Niidome, T.2    Kimura, M.3    Hatakeyama, T.4    Aoyagi, H.5    Kurazono, H.6    Imagawa, K.7    Wada, A.8    Moss, J.9    Hirayama, T.10
  • 30
    • 0033542796 scopus 로고    scopus 로고
    • Phosphacan immunoreactivity is associated with perineuronal nets around parvalbumin-expressing neurones
    • [CrossRef]
    • Haunso, A.; Celio, M.R.; Margolis, R.K.; Menoud, P.A. Phosphacan immunoreactivity is associated with perineuronal nets around parvalbumin-expressing neurones. Brain Res. 1999, 834, 219-222. [CrossRef]
    • (1999) Brain Res. , vol.834 , pp. 219-222
    • Haunso, A.1    Celio, M.R.2    Margolis, R.K.3    Menoud, P.A.4
  • 31
    • 0029834975 scopus 로고    scopus 로고
    • 6B4 proteoglycan/phosphacan, an extracellular variant of receptor-like protein-tyrosine phosphatase zeta/RPTPbeta, binds pleiotrophin/heparin-binding growth-associated molecule (HB-GAM)
    • [PubMed]
    • Maeda, N.; Nishiwaki, T.; Shintani, T.; Hamanaka, H.; Noda, M. 6B4 proteoglycan/phosphacan, an extracellular variant of receptor-like protein-tyrosine phosphatase zeta/RPTPbeta, binds pleiotrophin/heparin-binding growth-associated molecule (HB-GAM). J. Biol. Chem. 1996, 271, 21446-21452. [PubMed]
    • (1996) J. Biol. Chem. , vol.271 , pp. 21446-21452
    • Maeda, N.1    Nishiwaki, T.2    Shintani, T.3    Hamanaka, H.4    Noda, M.5
  • 32
    • 0030043021 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans in the developing central nervous system. II. Immunocytochemical localization of neurocan and phosphacan
    • [CrossRef]
    • Meyer-Puttlitz, B.; Junker, E.; Margolis, R.U.; Margolis, R.K. Chondroitin sulfate proteoglycans in the developing central nervous system. II. Immunocytochemical localization of neurocan and phosphacan. J. Comp. Neurol. 1996, 366, 44-54. [CrossRef]
    • (1996) J. Comp. Neurol. , vol.366 , pp. 44-54
    • Meyer-Puttlitz, B.1    Junker, E.2    Margolis, R.U.3    Margolis, R.K.4
  • 33
    • 0041346429 scopus 로고    scopus 로고
    • Expression of midkine and receptor-like protein tyrosine phosphatase (RPTP)-beta genes in the rat stomach and the influence of rebamipide
    • [CrossRef] [PubMed]
    • Yuki, T.; Ishihara, S.; Rumi, M.; Ortega-Cava Cesar, F.; Kadowaki, Y.; Kazumori, H.; Yuki, M.; Wada, T.; Miyaoka, Y.; Yoshino, N.; et al. Expression of midkine and receptor-like protein tyrosine phosphatase (RPTP)-beta genes in the rat stomach and the influence of rebamipide. Aliment. Pharmacol. Ther. 2003, 18 (Suppl. 1), 106-112. [CrossRef] [PubMed]
    • (2003) Aliment. Pharmacol. Ther. , vol.18 , pp. 106-112
    • Yuki, T.1    Ishihara, S.2    Rumi, M.3    Ortega-Cava Cesar, F.4    Kadowaki, Y.5    Kazumori, H.6    Yuki, M.7    Wada, T.8    Miyaoka, Y.9    Yoshino, N.10
  • 34
    • 0037370481 scopus 로고    scopus 로고
    • Mice deficient in protein tyrosine phosphatase receptor type Z are resistant to gastric ulcer induction by VacA of Helicobacter pylori
    • [CrossRef] [PubMed]
    • Fujikawa, A.; Shirasaka, D.; Yamamoto, S.; Ota, H.; Yahiro, K.; Fukada, M.; Shintani, T.;Wada, A.; Aoyama, N.; Hirayama, T.; et al. Mice deficient in protein tyrosine phosphatase receptor type Z are resistant to gastric ulcer induction by VacA of Helicobacter pylori. Nat. Genet. 2003, 33, 375-381. [CrossRef] [PubMed]
    • (2003) Nat. Genet. , vol.33 , pp. 375-381
    • Fujikawa, A.1    Shirasaka, D.2    Yamamoto, S.3    Ota, H.4    Yahiro, K.5    Fukada, M.6    Shintani, T.7    Wada, A.8    Aoyama, N.9    Hirayama, T.10
  • 37
    • 33745107561 scopus 로고    scopus 로고
    • Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development
    • [CrossRef] [PubMed]
    • Baumer, S.; Keller, L.; Holtmann, A.; Funke, R.; August, B.; Gamp, A.;Wolburg, H.;Wolburg-Buchholz, K.; Deutsch, U.; Vestweber, D. Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development. Blood 2006, 107, 4754-4762. [CrossRef] [PubMed]
    • (2006) Blood , vol.107 , pp. 4754-4762
    • Baumer, S.1    Keller, L.2    Holtmann, A.3    Funke, R.4    August, B.5    Wolburg, A.6    Wolburg-Buchholz, H.7    Gamp, K.8    Deutsch, U.9    Vestweber, D.10
  • 38
    • 0032475902 scopus 로고    scopus 로고
    • Tpa and butyrate increase cell sensitivity to the vacuolating toxin of Helicobacter pylori
    • [CrossRef]
    • De Bernard, M.; Moschioni, M.; Papini, E.; Telford, J.L.; Rappuoli, R.; Montecucco, C. Tpa and butyrate increase cell sensitivity to the vacuolating toxin of Helicobacter pylori. FEBS Lett. 1998, 436, 218-222. [CrossRef]
    • (1998) FEBS Lett. , vol.436 , pp. 218-222
    • De Bernard, M.1    Moschioni, M.2    Papini, E.3    Telford, J.L.4    Rappuoli, R.5    Montecucco, C.6
  • 39
    • 0034686079 scopus 로고    scopus 로고
    • Morphologic differentiation of HL-60 cells is associated with appearance of RPTPbeta and induction of Helicobacter pylori VacA sensitivity
    • [CrossRef] [PubMed]
    • Padilla, P.I.;Wada, A.; Yahiro, K.; Kimura, M.; Niidome, T.; Aoyagi, H.; Kumatori, A.; Anami, M.; Hayashi, T.; Fujisawa, J.; et al. Morphologic differentiation of HL-60 cells is associated with appearance of RPTPbeta and induction of Helicobacter pylori VacA sensitivity. J. Biol. Chem. 2000, 275, 15200-15206. [CrossRef] [PubMed]
    • (2000) J. Biol. Chem. , vol.275 , pp. 15200-15206
    • Padilla, P.I.1    Yahiro, K.2    Kimura, M.3    Niidome, T.4    Aoyagi, H.5    Kumatori, A.6    Anami, M.7    Hayashi, T.8    Fujisawa, J.9
  • 40
    • 19944421388 scopus 로고    scopus 로고
    • Essential domain of receptor tyrosine phosphatase beta (RPTPbeta) for interaction with Helicobacter pylori vacuolating cytotoxin
    • [CrossRef] [PubMed]
    • Yahiro, K.; Wada, A.; Yamasaki, E.; Nakayama, M.; Nishi, Y.; Hisatsune, J.; Morinaga, N.; Sap, J.; Noda, M.; Moss, J.; et al. Essential domain of receptor tyrosine phosphatase beta (RPTPbeta) for interaction with Helicobacter pylori vacuolating cytotoxin. J. Biol. Chem. 2004, 279, 51013-51021. [CrossRef] [PubMed]
    • (2004) J. Biol. Chem. , vol.279 , pp. 51013-51021
    • Yahiro, K.1    Wada, A.2    Yamasaki, E.3    Nakayama, M.4    Nishi, Y.5    Hisatsune, J.6    Morinaga, N.7    Sap, J.8    Noda, M.9    Moss, J.10
  • 41
    • 84936985148 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 285 of PAK1 facilitates βPIX/GIT1 binding and adhesion turnover
    • [CrossRef] [PubMed]
    • Hammer, A.; Oladimeji, P.; De Las Casas, L.E.; Diakonova, M. Phosphorylation of tyrosine 285 of PAK1 facilitates βPIX/GIT1 binding and adhesion turnover. FASEB J. 2015, 29, 943-959. [CrossRef] [PubMed]
    • (2015) FASEB J. , vol.29 , pp. 943-959
    • Hammer, A.1    Oladimeji, P.2    De Las Casas, L.E.3    Diakonova, M.4
  • 42
    • 0025376471 scopus 로고
    • Identification of an additional member of the protein-tyrosine-phosphatase family: Evidence for alternative splicing in the tyrosine phosphatase domain
    • [CrossRef] [PubMed]
    • Matthews, R.J.; Cahir, E.D.; Thomas, M.L. Identification of an additional member of the protein-tyrosine-phosphatase family: Evidence for alternative splicing in the tyrosine phosphatase domain. Proc. Natl. Acad. Sci. USA 1990, 87, 4444-4448. [CrossRef] [PubMed]
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4444-4448
    • Matthews, R.J.1    Cahir, E.D.2    Thomas, M.L.3
  • 43
    • 0025073036 scopus 로고
    • Cloning and expression of a widely expressed receptor tyrosine phosphatase
    • [CrossRef] [PubMed]
    • Sap, J.; D’Eustachio, P.; Givol, D.; Schlessinger, J. Cloning and expression of a widely expressed receptor tyrosine phosphatase. Proc. Natl. Acad. Sci. USA 1990, 87, 6112-6116. [CrossRef] [PubMed]
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6112-6116
    • Sap, J.1    D’Eustachio, P.2    Givol, D.3    Schlessinger, J.4
  • 45
    • 84901803023 scopus 로고    scopus 로고
    • RPTPalpha controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin
    • [CrossRef] [PubMed]
    • Truffi, M.; Dubreuil, V.; Liang, X.; Vacaresse, N.; Nigon, F.; Han, S.P.; Yap, A.S.; Gomez, G.A.; Sap, J. RPTPalpha controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin. J. Cell Sci. 2014, 127, 2420-2432. [CrossRef] [PubMed]
    • (2014) J. Cell Sci. , vol.127 , pp. 2420-2432
    • Truffi, M.1    Dubreuil, V.2    Liang, X.3    Vacaresse, N.4    Nigon, F.5    Han, S.P.6    Yap, A.S.7    Gomez, G.A.8    Sap, J.9
  • 46
    • 84926430034 scopus 로고    scopus 로고
    • An RPTPalpha/Src family kinase/RAP1 signaling module recruits myosin IIB to support contractile tension at apical E-cadherin junctions
    • [CrossRef] [PubMed]
    • Gomez, G.A.; McLachlan, R.W.; Wu, S.K.; Caldwell, B.J.; Moussa, E.; Verma, S.; Bastiani, M.; Priya, R.; Parton, R.G.; Gaus, K.; et al. An RPTPalpha/Src family kinase/RAP1 signaling module recruits myosin IIB to support contractile tension at apical E-cadherin junctions. Mol. Biol. Cell 2015, 26, 1249-1262. [CrossRef] [PubMed]
    • (2015) Mol. Biol. Cell , vol.26 , pp. 1249-1262
    • Gomez, G.A.1    McLachlan, R.W.2    Wu, S.K.3    Caldwell, B.J.4    Moussa, E.5    Verma, S.6    Bastiani, M.7    Priya, R.8    Parton, R.G.9    Gaus, K.10
  • 47
    • 0032802253 scopus 로고    scopus 로고
    • The mammalian low-density lipoprotein receptor family
    • [CrossRef] [PubMed]
    • Hussain, M.M.; Strickland, D.K.; Bakillah, A. The mammalian low-density lipoprotein receptor family. Ann. Rev. Nutr. 1999, 19, 141-172. [CrossRef] [PubMed]
    • (1999) Ann. Rev. Nutr. , vol.19 , pp. 141-172
    • Hussain, M.M.1    Strickland, D.K.2    Bakillah, A.3
  • 49
    • 0037373880 scopus 로고    scopus 로고
    • Induction of gastric epithelial cell apoptosis by Helicobacter pylori vacuolating cytotoxin
    • [PubMed]
    • Cover, T.L.; Krishna, U.S.; Israel, D.A.; Peek, R.M., Jr. Induction of gastric epithelial cell apoptosis by Helicobacter pylori vacuolating cytotoxin. Cancer Res. 2003, 63, 951-957. [PubMed]
    • (2003) Cancer Res. , vol.63 , pp. 951-957
    • Cover, T.L.1    Krishna, U.S.2    Israel, D.A.3    Peek, R.M.4
  • 50
    • 1642431978 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin enters cells, localizes to the mitochondria, and induces mitochondrial membrane permeability changes correlated to toxin channel activity
    • [CrossRef] [PubMed]
    • Willhite, D.C.; Blanke, S.R. Helicobacter pylori vacuolating cytotoxin enters cells, localizes to the mitochondria, and induces mitochondrial membrane permeability changes correlated to toxin channel activity. Cell. Microbiol. 2004, 6, 143-154. [CrossRef] [PubMed]
    • (2004) Cell. Microbiol. , vol.6 , pp. 143-154
    • Willhite, D.C.1    Blanke, S.R.2
  • 51
    • 33744960020 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin induces activation of the proapoptotic proteins bax and bak, leading to cytochrome c release and cell death, independent of vacuolation
    • [CrossRef] [PubMed]
    • Yamasaki, E.; Wada, A.; Kumatori, A.; Nakagawa, I.; Funao, J.; Nakayama, M.; Hisatsune, J.; Kimura, M.; Moss, J.; Hirayama, T. Helicobacter pylori vacuolating cytotoxin induces activation of the proapoptotic proteins bax and bak, leading to cytochrome c release and cell death, independent of vacuolation. J. Biol. Chem. 2006, 281, 11250-11259. [CrossRef] [PubMed]
    • (2006) J. Biol. Chem. , vol.281 , pp. 11250-11259
    • Yamasaki, E.1    Wada, A.2    Kumatori, A.3    Nakagawa, I.4    Funao, J.5    Nakayama, M.6    Hisatsune, J.7    Kimura, M.8    Moss, J.9    Hirayama, T.10
  • 52
    • 0034923765 scopus 로고    scopus 로고
    • Vacuolating cytotoxin of Helicobacter pylori induces apoptosis in the human gastric epithelial cell line ags
    • [CrossRef] [PubMed]
    • Kuck, D.; Kolmerer, B.; Iking-Konert, C.; Krammer, P.H.; Stremmel, W.; Rudi, J. Vacuolating cytotoxin of Helicobacter pylori induces apoptosis in the human gastric epithelial cell line ags. Infect. Immun. 2001, 69, 5080-5087. [CrossRef] [PubMed]
    • (2001) Infect. Immun. , vol.69 , pp. 5080-5087
    • Kuck, D.1    Kolmerer, B.2    Iking-Konert, C.3    Krammer, P.H.4    Stremmel, W.5    Rudi, J.6
  • 53
    • 0034388020 scopus 로고    scopus 로고
    • The N-terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release
    • [CrossRef] [PubMed]
    • Galmiche, A.; Rassow, J.; Doye, A.; Cagnol, S.; Chambard, J.C.; Contamin, S.; de Thillot, V.; Just, I.; Ricci, V.; Solcia, E.; et al. The N-terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release. EMBO J. 2000, 19, 6361-6370. [CrossRef] [PubMed]
    • (2000) EMBO J. , vol.19 , pp. 6361-6370
    • Galmiche, A.1    Rassow, J.2    Doye, A.3    Cagnol, S.4    Chambard, J.C.5    Contamin, S.6    De Thillot, V.7    Just, I.8    Ricci, V.9    Solcia, E.10
  • 55
    • 80053139817 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin A (VacA) engages the mitochondrial fission machinery to induce host cell death
    • [CrossRef] [PubMed]
    • Jain, P.; Luo, Z.Q.; Blanke, S.R. Helicobacter pylori vacuolating cytotoxin A (VacA) engages the mitochondrial fission machinery to induce host cell death. Proc. Natl. Acad. Sci. USA 2011, 108, 16032-16037. [CrossRef] [PubMed]
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 16032-16037
    • Jain, P.1    Luo, Z.Q.2    Blanke, S.R.3
  • 56
    • 79959476135 scopus 로고    scopus 로고
    • Helicobacter pylori VacA induces programmed necrosis in gastric epithelial cells
    • [CrossRef] [PubMed]
    • Radin, J.N.; Gonzalez-Rivera, C.; Ivie, S.E.; McClain, M.S.; Cover, T.L. Helicobacter pylori VacA induces programmed necrosis in gastric epithelial cells. Infect. Immun. 2011, 79, 2535-2543. [CrossRef] [PubMed]
    • (2011) Infect. Immun. , vol.79 , pp. 2535-2543
    • Radin, J.N.1    Gonzalez-Rivera, C.2    Ivie, S.E.3    McClain, M.S.4    Cover, T.L.5
  • 57
    • 84896078858 scopus 로고    scopus 로고
    • Helicobacter pylori caga and gastric cancer: A paradigm for hit-and-run carcinogenesis
    • [CrossRef] [PubMed]
    • Hatakeyama, M. Helicobacter pylori caga and gastric cancer: A paradigm for hit-and-run carcinogenesis. Cell Host Microbe 2014, 15, 306-316. [CrossRef] [PubMed]
    • (2014) Cell Host Microbe , vol.15 , pp. 306-316
    • Hatakeyama, M.1
  • 58
    • 84870999066 scopus 로고    scopus 로고
    • Reactive oxygen species-induced autophagic degradation of Helicobacter pylori CagA is specifically suppressed in cancer stem-like cells
    • [CrossRef] [PubMed]
    • Tsugawa, H.; Suzuki, H.; Saya, H.; Hatakeyama, M.; Hirayama, T.; Hirata, K.; Nagano, O.; Matsuzaki, J.; Hibi, T. Reactive oxygen species-induced autophagic degradation of Helicobacter pylori CagA is specifically suppressed in cancer stem-like cells. Cell Host Microbe 2012, 12, 764-777. [CrossRef] [PubMed]
    • (2012) Cell Host Microbe , vol.12 , pp. 764-777
    • Tsugawa, H.1    Suzuki, H.2    Saya, H.3    Hatakeyama, M.4    Hirayama, T.5    Hirata, K.6    Nagano, O.7    Matsuzaki, J.8    Hibi, T.9
  • 59
    • 0032563331 scopus 로고    scopus 로고
    • Vacuolation induced by cytotoxin from Helicobacter pylori is mediated by the EGF receptor in hela cells
    • [CrossRef]
    • Seto, K.; Hayashi-Kuwabara, Y.; Yoneta, T.; Suda, H.; Tamaki, H. Vacuolation induced by cytotoxin from Helicobacter pylori is mediated by the EGF receptor in hela cells. FEBS Lett. 1998, 431, 347-350. [CrossRef]
    • (1998) FEBS Lett. , vol.431 , pp. 347-350
    • Seto, K.1    Hayashi-Kuwabara, Y.2    Yoneta, T.3    Suda, H.4    Tamaki, H.5
  • 60
    • 0347132270 scopus 로고    scopus 로고
    • Helicobacter pylori infection inhibits healing of the wounded duodenal epithelium in vitro
    • [CrossRef] [PubMed]
    • Tabel, G.; Hoa, N.T.; Tarnawski, A.; Chen, J.; Domek, M.; Ma, T.Y. Helicobacter pylori infection inhibits healing of the wounded duodenal epithelium in vitro. J. Lab. Clin. Med. 2003, 142, 421-430. [CrossRef] [PubMed]
    • (2003) J. Lab. Clin. Med. , vol.142 , pp. 421-430
    • Tabel, G.1    Hoa, N.T.2    Tarnawski, A.3    Chen, J.4    Domek, M.5    Ma, T.Y.6
  • 61
    • 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
    • [CrossRef] [PubMed]
    • Tegtmeyer, N.; Zabler, D.; Schmidt, D.; Hartig, R.; Brandt, S.; Backert, S. 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. Cell. Microbiol. 2009, 11, 488-505. [CrossRef] [PubMed]
    • (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
  • 62
    • 84896392867 scopus 로고    scopus 로고
    • Multiscale relationships between fibronectin structure and functional properties
    • [PubMed]
    • Bradshaw, M.J.; Smith, M.L. Multiscale relationships between fibronectin structure and functional properties. Acta Biomater. 2014, 10, 1524-1531. [PubMed]
    • (2014) Acta Biomater. , vol.10 , pp. 1524-1531
    • Bradshaw, M.J.1    Smith, M.L.2
  • 64
    • 0037452070 scopus 로고    scopus 로고
    • Microbial pathogenesis and cytoskeletal function
    • [PubMed]
    • Gruenheid, S.; Finlay, B.B. Microbial pathogenesis and cytoskeletal function. Nature 2003, 422, 775-781. [PubMed]
    • (2003) Nature , vol.422 , pp. 775-781
    • Gruenheid, S.1    Finlay, B.B.2
  • 65
    • 24344483178 scopus 로고    scopus 로고
    • Helicobacter pylori VacA cytotoxin interacts with fibronectin and alters hela cell adhesion and cytoskeletal organization in vitro
    • [CrossRef] [PubMed]
    • Hennig, E.E.; Godlewski, M.M.; Butruk, E.; Ostrowski, J. Helicobacter pylori VacA cytotoxin interacts with fibronectin and alters hela cell adhesion and cytoskeletal organization in vitro. FEMS Immunol. Med. Microbiol. 2005, 44, 143-150. [CrossRef] [PubMed]
    • (2005) FEMS Immunol. Med. Microbiol. , vol.44 , pp. 143-150
    • Hennig, E.E.1    Godlewski, M.M.2    Butruk, E.3    Ostrowski, J.4
  • 66
    • 0033584434 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin (VacA) disorganizes the cytoskeletal architecture of gastric epithelial cells
    • [CrossRef] [PubMed]
    • Pai, R.; Cover, T.L.; Tarnawski, A.S. Helicobacter pylori vacuolating cytotoxin (VacA) disorganizes the cytoskeletal architecture of gastric epithelial cells. Biochem. Biophys. Res. Commun. 1999, 262, 245-250. [CrossRef] [PubMed]
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 245-250
    • Pai, R.1    Cover, T.L.2    Tarnawski, A.S.3
  • 67
    • 0035068436 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin binding to a putative cell surface receptor, heparan sulfate, studied by surface plasmon resonance
    • [CrossRef] [PubMed]
    • Utt, M.; Danielsson, B.; Wadstrom, T. Helicobacter pylori vacuolating cytotoxin binding to a putative cell surface receptor, heparan sulfate, studied by surface plasmon resonance. FEMS Immunol. Med. Microbiol. 2001, 30, 109-113. [CrossRef] [PubMed]
    • (2001) FEMS Immunol. Med. Microbiol. , vol.30 , pp. 109-113
    • Utt, M.1    Danielsson, B.2    Wadstrom, T.3
  • 68
    • 65349185031 scopus 로고    scopus 로고
    • Lrp-1: A new modulator of cytoskeleton dynamics and adhesive complex turnover in cancer cells
    • [CrossRef]
    • Dedieu, S.; Langlois, B. Lrp-1: A new modulator of cytoskeleton dynamics and adhesive complex turnover in cancer cells. Cell Adhes. Migr. 2008, 2, 77-80. [CrossRef]
    • (2008) Cell Adhes. Migr. , vol.2 , pp. 77-80
    • Dedieu, S.1    Langlois, B.2
  • 69
    • 4344690860 scopus 로고    scopus 로고
    • Targeting of Helicobacter pylori vacuolating toxin to lipid raft membrane domains analysed by atomic force microscopy
    • [CrossRef] [PubMed]
    • Geisse, N.A.; Cover, T.L.; Henderson, R.M.; Edwardson, J.M. Targeting of Helicobacter pylori vacuolating toxin to lipid raft membrane domains analysed by atomic force microscopy. Biochem. J. 2004, 381, 911-917. [CrossRef] [PubMed]
    • (2004) Biochem. J. , vol.381 , pp. 911-917
    • Geisse, N.A.1    Cover, T.L.2    Henderson, R.M.3    Edwardson, J.M.4
  • 70
    • 0037072947 scopus 로고    scopus 로고
    • Association of Helicobacter pylori vacuolating toxin (VacA) with lipid rafts
    • [CrossRef] [PubMed]
    • Schraw,W.; Li, Y.; McClain, M.S.; van der Goot, F.G.; Cover, T.L. Association of Helicobacter pylori vacuolating toxin (VacA) with lipid rafts. J. Biol. Chem. 2002, 277, 34642-34650. [CrossRef] [PubMed]
    • (2002) J. Biol. Chem. , vol.277 , pp. 34642-34650
    • Schraw, W.1    Li, Y.2    McClain, M.S.3    Van Der Goot, F.G.4    Cover, T.L.5
  • 71
    • 0036073382 scopus 로고    scopus 로고
    • Plasma membrane cholesterol modulates cellular vacuolation induced by the Helicobacter pylori vacuolating cytotoxin
    • [CrossRef] [PubMed]
    • Patel, H.K.; Willhite, D.C.; Patel, R.M.; Ye, D.; Williams, C.L.; Torres, E.M.; Marty, K.B.; MacDonald, R.A.; Blanke, S.R. Plasma membrane cholesterol modulates cellular vacuolation induced by the Helicobacter pylori vacuolating cytotoxin. Infect. Immun. 2002, 70, 4112-4123. [CrossRef] [PubMed]
    • (2002) Infect. Immun. , vol.70 , pp. 4112-4123
    • Patel, H.K.1    Willhite, D.C.2    Patel, R.M.3    Ye, D.4    Williams, C.L.5    Torres, E.M.6    Marty, K.B.7    MacDonald, R.A.8    Blanke, S.R.9
  • 72
    • 0037418698 scopus 로고    scopus 로고
    • Binding and internalization of Helicobacter pylori VacA via cellular lipid rafts in epithelial cells
    • [CrossRef]
    • Kuo, C.H.; Wang, W.C. Binding and internalization of Helicobacter pylori VacA via cellular lipid rafts in epithelial cells. Biochem. Biophys. Res. Commun. 2003, 303, 640-644. [CrossRef]
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 640-644
    • Kuo, C.H.1    Wang, W.C.2
  • 73
    • 33845503473 scopus 로고    scopus 로고
    • Clustering of Helicobacter pylori VacA in lipid rafts, mediated by its receptor, receptor-like protein tyrosine phosphatase beta, is required for intoxication in AZ-521 cells
    • [CrossRef] [PubMed]
    • Nakayama, M.; Hisatsune, J.; Yamasaki, E.; Nishi, Y.;Wada, A.; Kurazono, H.; Sap, J.; Yahiro, K.; Moss, J.; Hirayama, T. Clustering of Helicobacter pylori VacA in lipid rafts, mediated by its receptor, receptor-like protein tyrosine phosphatase beta, is required for intoxication in AZ-521 cells. Infect. Immun. 2006, 74, 6571-6580. [CrossRef] [PubMed]
    • (2006) Infect. Immun. , vol.74 , pp. 6571-6580
    • Nakayama, M.1    Hisatsune, J.2    Yamasaki, E.3    Nishi, Y.4    Kurazono, H.5    Sap, J.6    Yahiro, K.7    Moss, J.8    Hirayama, T.9
  • 74
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • [CrossRef] [PubMed]
    • Pike, L.J. Lipid rafts: Bringing order to chaos. J. Lipid Res. 2003, 44, 655-667. [CrossRef] [PubMed]
    • (2003) J. Lipid Res. , vol.44 , pp. 655-667
    • Pike, L.J.1
  • 75
    • 0033748047 scopus 로고    scopus 로고
    • High cell sensitivity to Helicobacter pylori VacA toxin depends on a GPI-anchored protein and is not blocked by inhibition of the clathrin-mediated pathway of endocytosis
    • [CrossRef] [PubMed]
    • Ricci, V.; Galmiche, A.; Doye, A.; Necchi, V.; Solcia, E.; Boquet, P. High cell sensitivity to Helicobacter pylori VacA toxin depends on a GPI-anchored protein and is not blocked by inhibition of the clathrin-mediated pathway of endocytosis. Mol. Biol. Cell 2000, 11, 3897-3909. [CrossRef] [PubMed]
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3897-3909
    • Ricci, V.1    Galmiche, A.2    Doye, A.3    Necchi, V.4    Solcia, E.5    Boquet, P.6
  • 77
    • 0033515072 scopus 로고    scopus 로고
    • The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low ph
    • [CrossRef] [PubMed]
    • Czajkowsky, D.M.; Iwamoto, H.; Cover, T.L.; Shao, Z. The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low ph. Proc. Natl. Acad. Sci. USA 1999, 96, 2001-2006. [CrossRef] [PubMed]
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2001-2006
    • Czajkowsky, D.M.1    Iwamoto, H.2    Cover, T.L.3    Shao, Z.4
  • 78
    • 78249272018 scopus 로고    scopus 로고
    • Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA
    • [CrossRef] [PubMed]
    • Gupta, V.R.;Wilson, B.A.; Blanke, S.R. Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA. Cell. Microbiol. 2010, 12, 1517-1533. [CrossRef] [PubMed]
    • (2010) Cell. Microbiol. , vol.12 , pp. 1517-1533
    • Gupta, V.R.1    Blanke, S.R.2
  • 79
    • 0033635310 scopus 로고    scopus 로고
    • Heparin and heparan sulfate: Biosynthesis, structure and function
    • [CrossRef]
    • Sasisekharan, R.; Venkataraman, G. Heparin and heparan sulfate: Biosynthesis, structure and function. Curr. Opin. Chem. Biol. 2000, 4, 626-631. [CrossRef]
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 626-631
    • Sasisekharan, R.1    Venkataraman, G.2
  • 81
    • 0033617313 scopus 로고    scopus 로고
    • A receptor-like protein-tyrosine phosphatase ptpzeta/rptpbeta binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to ptpzeta
    • [CrossRef] [PubMed]
    • Maeda, N.; Ichihara-Tanaka, K.; Kimura, T.; Kadomatsu, K.; Muramatsu, T.; Noda, M. A receptor-like protein-tyrosine phosphatase ptpzeta/rptpbeta binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to ptpzeta. J. Biol. Chem. 1999, 274, 12474-12479. [CrossRef] [PubMed]
    • (1999) J. Biol. Chem. , vol.274 , pp. 12474-12479
    • Maeda, N.1    Ichihara-Tanaka, K.2    Kimura, T.3    Kadomatsu, K.4    Muramatsu, T.5    Noda, M.6
  • 82
    • 0031974233 scopus 로고    scopus 로고
    • Selective inhibition of ii-dependent antigen presentation by Helicobacter pylori toxin VacA
    • [CrossRef] [PubMed]
    • Molinari, M.; Salio, M.; Galli, C.; Norais, N.; Rappuoli, R.; Lanzavecchia, A.; Montecucco, C. Selective inhibition of ii-dependent antigen presentation by Helicobacter pylori toxin VacA. J. Exp. Med. 1998, 187, 135-140. [CrossRef] [PubMed]
    • (1998) J. Exp. Med. , vol.187 , pp. 135-140
    • Molinari, M.1    Salio, M.2    Galli, C.3    Norais, N.4    Rappuoli, R.5    Lanzavecchia, A.6    Montecucco, C.7
  • 83
    • 38049076855 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits activation-induced proliferation of human T and B lymphocyte subsets
    • [CrossRef] [PubMed]
    • Torres, V.J.; vanCompernolle, S.E.; Sundrud, M.S.; Unutmaz, D.; Cover, T.L. Helicobacter pylori vacuolating cytotoxin inhibits activation-induced proliferation of human T and B lymphocyte subsets. J. Immunol. 2007, 179, 5433-5440. [CrossRef] [PubMed]
    • (2007) J. Immunol. , vol.179 , pp. 5433-5440
    • Torres, V.J.1    VanCompernolle, S.E.2    Sundrud, M.S.3    Unutmaz, D.4    Cover, T.L.5
  • 84
    • 0042932364 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits t lymphocyte activation
    • [CrossRef] [PubMed]
    • Gebert, B.; Fischer,W.;Weiss, E.; Hoffmann, R.; Haas, R. Helicobacter pylori vacuolating cytotoxin inhibits t lymphocyte activation. Science 2003, 301, 1099-1102. [CrossRef] [PubMed]
    • (2003) Science , vol.301 , pp. 1099-1102
    • Gebert, B.1    Fischer, W.2    Hoffmann, R.3    Haas, R.4
  • 86
    • 2442682964 scopus 로고    scopus 로고
    • Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion
    • [CrossRef] [PubMed]
    • Sundrud, M.S.; Torres, V.J.; Unutmaz, D.; Cover, T.L. Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion. Proc. Natl. Acad. Sci. USA 2004, 101, 7727-7732. [CrossRef] [PubMed]
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7727-7732
    • Sundrud, M.S.1    Torres, V.J.2    Unutmaz, D.3    Cover, T.L.4
  • 88
    • 79951487830 scopus 로고    scopus 로고
    • Pkc-dependent endocytosis of the Helicobacter pylori vacuolating cytotoxin in primary T lymphocytes
    • [CrossRef] [PubMed]
    • Sewald, X.; Jimenez-Soto, L.; Haas, R. Pkc-dependent endocytosis of the Helicobacter pylori vacuolating cytotoxin in primary T lymphocytes. Cell. Microbiol. 2011, 13, 482-496. [CrossRef] [PubMed]
    • (2011) Cell. Microbiol. , vol.13 , pp. 482-496
    • Sewald, X.1    Jimenez-Soto, L.2    Haas, R.3
  • 89
    • 84864820769 scopus 로고    scopus 로고
    • The intermediate region of Helicobacter pylori VacA is a determinant of toxin potency in a jurkat T cell assay
    • [CrossRef] [PubMed]
    • Gonzalez-Rivera, C.; Algood, H.M.; Radin, J.N.; McClain, M.S.; Cover, T.L. The intermediate region of Helicobacter pylori VacA is a determinant of toxin potency in a jurkat T cell assay. Infect. Immun. 2012, 80, 2578-2588. [CrossRef] [PubMed]
    • (2012) Infect. Immun. , vol.80 , pp. 2578-2588
    • Gonzalez-Rivera, C.1    Algood, H.M.2    Radin, J.N.3    McClain, M.S.4    Cover, T.L.5
  • 90
    • 34548495047 scopus 로고    scopus 로고
    • A new Helicobacter pylori vacuolating cytotoxin determinant, the intermediate region, is associated with gastric cancer
    • [CrossRef] [PubMed]
    • Rhead, J.L.; Letley, D.P.; Mohammadi, M.; Hussein, N.; Mohagheghi, M.A.; Eshagh Hosseini, M.; Atherton, J.C. A new Helicobacter pylori vacuolating cytotoxin determinant, the intermediate region, is associated with gastric cancer. Gastroenterology 2007, 133, 926-936. [CrossRef] [PubMed]
    • (2007) Gastroenterology , vol.133 , pp. 926-936
    • Rhead, J.L.1    Letley, D.P.2    Mohammadi, M.3    Hussein, N.4    Mohagheghi, M.A.5    Eshagh Hosseini, M.6    Atherton, J.C.7
  • 91
    • 80052635374 scopus 로고    scopus 로고
    • Stimulation of dendritic cells with Helicobacter pylori vacuolating cytotoxin negatively regulates their maturation via the restoration of E2F1
    • [CrossRef] [PubMed]
    • Kim, J.M.; Kim, J.S.; Yoo, D.Y.; Ko, S.H.; Kim, N.; Kim, H.; Kim, Y.J. Stimulation of dendritic cells with Helicobacter pylori vacuolating cytotoxin negatively regulates their maturation via the restoration of E2F1. Clin. Exp. Immunol. 2011, 166, 34-45. [CrossRef] [PubMed]
    • (2011) Clin. Exp. Immunol. , vol.166 , pp. 34-45
    • Kim, J.M.1    Kim, J.S.2    Yoo, D.Y.3    Ko, S.H.4    Kim, N.5    Kim, H.6    Kim, Y.J.7
  • 93
    • 33745588616 scopus 로고    scopus 로고
    • Platelet activation in Helicobacter pylori-associated idiopathic thrombocytopenic purpura: Eradication reduces platelet activation but seldom improves platelet counts
    • [CrossRef] [PubMed]
    • Ahn, E.R.; Tiede, M.P.; Jy, W.; Bidot, C.J.; Fontana, V.; Ahn, Y.S. Platelet activation in Helicobacter pylori-associated idiopathic thrombocytopenic purpura: Eradication reduces platelet activation but seldom improves platelet counts. Acta Haematol. 2006, 116, 19-24. [CrossRef] [PubMed]
    • (2006) Acta Haematol. , vol.116 , pp. 19-24
    • Ahn, E.R.1    Tiede, M.P.2    Jy, W.3    Bidot, C.J.4    Fontana, V.5    Ahn, Y.S.6
  • 94
    • 0033857204 scopus 로고    scopus 로고
    • Production and characterization of monoclonal antibodies against conserved epitopes of P-selectin (CD62P)
    • [CrossRef] [PubMed]
    • Massaguer, A.; Engel, P.; Perez-del-Pulgar, S.; Bosch, J.; Pizcueta, P. Production and characterization of monoclonal antibodies against conserved epitopes of P-selectin (CD62P). Tissue Antigens 2000, 56, 117-128. [CrossRef] [PubMed]
    • (2000) Tissue Antigens , vol.56 , pp. 117-128
    • Massaguer, A.1    Engel, P.2    Perez-Del-Pulgar, S.3    Bosch, J.4    Pizcueta, P.5
  • 95
    • 84887346964 scopus 로고    scopus 로고
    • VacA, the vacuolating cytotoxin of Helicobacter pylori, binds to multimerin 1 on human platelets
    • [CrossRef] [PubMed]
    • Satoh, K.; Hirayama, T.; Takano, K.; Suzuki-Inoue, K.; Sato, T.; Ohta, M.; Nakagomi, J.; Ozaki, Y. VacA, the vacuolating cytotoxin of Helicobacter pylori, binds to multimerin 1 on human platelets. Thromb. J. 2013, 11, 23. [CrossRef] [PubMed]
    • (2013) Thromb. J. , vol.11 , pp. 23
    • Satoh, K.1    Hirayama, T.2    Takano, K.3    Suzuki-Inoue, K.4    Sato, T.5    Ohta, M.6    Nakagomi, J.7    Ozaki, Y.8
  • 96
  • 97
    • 33644690335 scopus 로고    scopus 로고
    • Elucidation of N-glycosylation sites on human platelet proteins: A glycoproteomic approach
    • [CrossRef] [PubMed]
    • Lewandrowski, U.; Moebius, J.; Walter, U.; Sickmann, A. Elucidation of N-glycosylation sites on human platelet proteins: A glycoproteomic approach. Mol. Cell. Proteom. MCP 2006, 5, 226-233. [CrossRef] [PubMed]
    • (2006) Mol. Cell. Proteom. MCP , vol.5 , pp. 226-233
    • Lewandrowski, U.1    Moebius, J.2    Walter, U.3    Sickmann, A.4
  • 99
    • 63049084005 scopus 로고    scopus 로고
    • Platelet adhesion to multimerin 1 in vitro: Influences of platelet membrane receptors, von willebrand factor and shear
    • [CrossRef] [PubMed]
    • Tasneem, S.; Adam, F.; Minullina, I.; Pawlikowska, M.; Hui, S.K.; Zheng, S.; Miller, J.L.; Hayward, C.P. Platelet adhesion to multimerin 1 in vitro: Influences of platelet membrane receptors, von willebrand factor and shear. J. Thromb. Haemost. JTH 2009, 7, 685-692. [CrossRef] [PubMed]
    • (2009) J. Thromb. Haemost. JTH , vol.7 , pp. 685-692
    • Tasneem, S.1    Adam, F.2    Minullina, I.3    Pawlikowska, M.4    Hui, S.K.5    Zheng, S.6    Miller, J.L.7    Hayward, C.P.8
  • 100
    • 0028787845 scopus 로고
    • Microbial recognition of target-cell glycoconjugates
    • [CrossRef]
    • Karlsson, K.A. Microbial recognition of target-cell glycoconjugates. Curr. Opin. Struct. Biol. 1995, 5, 622-635. [CrossRef]
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 622-635
    • Karlsson, K.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.