메뉴 건너뛰기




Volumn 84, Issue 9, 2016, Pages 2662-2670

A nonoligomerizing mutant form of helicobacter pylori vaca allows structural analysis of the p33 domain

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEIN P33; PROTEIN P55; VACUOLATING TOXIN; BACTERIAL PROTEIN; BACTERIAL TOXIN; ION CHANNEL; VACA PROTEIN, HELICOBACTER PYLORI;

EID: 84984817886     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00254-16     Document Type: Article
Times cited : (19)

References (70)
  • 1
    • 70349211747 scopus 로고    scopus 로고
    • Coadaptation of Helicobacter pylori and humans: ancient history, modern implications
    • Atherton JC, Blaser MJ. 2009. Coadaptation of Helicobacter pylori and humans: ancient history, modern implications. J Clin Invest 119:2475-2487. http://dx.doi.org/10.1172/JCI38605.
    • (2009) J Clin Invest , vol.119 , pp. 2475-2487
    • Atherton, J.C.1    Blaser, M.J.2
  • 2
    • 65449190100 scopus 로고    scopus 로고
    • Helicobacter pylori in health and disease
    • Cover TL, Blaser MJ. 2009. Helicobacter pylori in health and disease. Gastroenterology 136:1863-1873. http://dx.doi.org/10.1053/j.gastro.2009.01.073.
    • (2009) Gastroenterology , vol.136 , pp. 1863-1873
    • Cover, T.L.1    Blaser, M.J.2
  • 3
    • 79952379428 scopus 로고    scopus 로고
    • Change is good: variations in common biological mechanisms in the epsilonproteobacterial genera Campylobacter and Helicobacter
    • Gilbreath JJ, Cody WL, Merrell DS, Hendrixson DR. 2011. Change is good: variations in common biological mechanisms in the epsilonproteobacterial genera Campylobacter and Helicobacter. Microbiol Mol Biol Rev 75:84-132. http://dx.doi.org/10.1128/MMBR.00035-10.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 84-132
    • Gilbreath, J.J.1    Cody, W.L.2    Merrell, D.S.3    Hendrixson, D.R.4
  • 4
    • 13444304088 scopus 로고    scopus 로고
    • Interaction of Helicobacter pylori with host cells: function of secreted and translocated molecules
    • Rieder G, Fischer W, Haas R. 2005. Interaction of Helicobacter pylori with host cells: function of secreted and translocated molecules. Curr Opin Microbiol 8:67-73. http://dx.doi.org/10.1016/j.mib.2004.12.004.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 67-73
    • Rieder, G.1    Fischer, W.2    Haas, R.3
  • 5
    • 84893734333 scopus 로고    scopus 로고
    • Structural and functional aspects of the Helicobacter pylori secretome
    • Zanotti G, Cendron L. 2014. Structural and functional aspects of the Helicobacter pylori secretome. World J Gastroenterol 20:1402-1423. http://dx.doi.org/10.3748/wjg.v20.i6.1402.
    • (2014) World J Gastroenterol , vol.20 , pp. 1402-1423
    • Zanotti, G.1    Cendron, L.2
  • 6
    • 84946422885 scopus 로고    scopus 로고
    • Growth phasedependent composition of the Helicobacter pylori exoproteome
    • Snider CA, Voss BJ, McDonald WH, Cover TL. 2016. Growth phasedependent composition of the Helicobacter pylori exoproteome. J Proteomics 130:94-107. http://dx.doi.org/10.1016/j.jprot.2015.08.025.
    • (2016) J Proteomics , vol.130 , pp. 94-107
    • Snider, C.A.1    Voss, B.J.2    McDonald, W.H.3    Cover, T.L.4
  • 7
    • 15944418287 scopus 로고    scopus 로고
    • Helicobacter pylori VacA, a paradigm for toxin multifunctionality
    • Cover TL, Blanke SR. 2005. Helicobacter pylori VacA, a paradigm for toxin multifunctionality. Nat Rev Microbiol 3:320-332. http://dx.doi.org/10.1038/nrmicro1095.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 320-332
    • Cover, T.L.1    Blanke, S.R.2
  • 8
    • 84859264679 scopus 로고    scopus 로고
    • Intoxication strategy of Helicobacter pylori VacA toxin
    • Boquet P, Ricci V. 2012. Intoxication strategy of Helicobacter pylori VacA toxin. Trends Microbiol 20:165-174. http://dx.doi.org/10.1016/j.tim.2012.01.008.
    • (2012) Trends Microbiol , vol.20 , pp. 165-174
    • Boquet, P.1    Ricci, V.2
  • 9
    • 84874711674 scopus 로고    scopus 로고
    • Remodeling the host environment: modulation of the gastric epithelium by the Helicobacter pylori vacuolating toxin (VacA)
    • Kim IJ, Blanke SR. 2012. Remodeling the host environment: modulation of the gastric epithelium by the Helicobacter pylori vacuolating toxin (VacA). Front Cell Infect Microbiol 2:37.
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 37
    • Kim, I.J.1    Blanke, S.R.2
  • 10
    • 84973483757 scopus 로고    scopus 로고
    • An overview of Helicobacter pylori VacA toxin biology
    • Foegeding NJ, Caston RR, McClain MS, Ohi MD, Cover TL. 2016. An overview of Helicobacter pylori VacA toxin biology. Toxins 8:173. http://dx .doi.org/10.3390/toxins8060173.
    • (2016) Toxins , vol.8 , pp. 173
    • Foegeding, N.J.1    Caston, R.R.2    McClain, M.S.3    Ohi, M.D.4    Cover, T.L.5
  • 11
    • 0023912268 scopus 로고
    • Cytotoxic activity in broth-culture filtrates of Campylobacter pylori
    • Leunk RD, Johnson PT, David BC, Kraft WG, Morgan DR. 1988. Cytotoxic activity in broth-culture filtrates of Campylobacter pylori. J Med Microbiol 26:93-99. http://dx.doi.org/10.1099/00222615-26-2-93.
    • (1988) J Med Microbiol , vol.26 , pp. 93-99
    • Leunk, R.D.1    Johnson, P.T.2    David, B.C.3    Kraft, W.G.4    Morgan, D.R.5
  • 12
    • 0026739795 scopus 로고
    • Purification and characterization of the vacuolating toxin from Helicobacter pylori
    • Cover TL, Blaser MJ. 1992. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J Biol Chem 267:10570-10575.
    • (1992) J Biol Chem , vol.267 , pp. 10570-10575
    • Cover, T.L.1    Blaser, M.J.2
  • 13
    • 0042932364 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation
    • Gebert B, Fischer W, Weiss E, Hoffman R, Haas R. 2003. Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation. Science 301:1099-1102. http://dx.doi.org/10.1126/science.1086871.
    • (2003) Science , vol.301 , pp. 1099-1102
    • Gebert, B.1    Fischer, W.2    Weiss, E.3    Hoffman, R.4    Haas, R.5
  • 15
    • 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
    • Sundrud MS, Torres VJ, Unutmaz D, Cover TL. 2004. 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 U S A 101:7727-7732. http://dx.doi.org/10.1073/pnas.0401528101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7727-7732
    • Sundrud, M.S.1    Torres, V.J.2    Unutmaz, D.3    Cover, T.L.4
  • 16
    • 38049076855 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits activationinduced proliferation of human T and B lymphocyte subsets
    • Torres VJ, Van Compernolle SE, Sundrud MS, Unutmaz D, Cover TL. 2007. Helicobacter pylori vacuolating cytotoxin inhibits activationinduced proliferation of human T and B lymphocyte subsets. J Immunol 179:5433-5440. http://dx.doi.org/10.4049/jimmunol.179.8.5433.
    • (2007) J Immunol , vol.179 , pp. 5433-5440
    • Torres, V.J.1    Van Compernolle, S.E.2    Sundrud, M.S.3    Unutmaz, D.4    Cover, T.L.5
  • 17
    • 0033515072 scopus 로고    scopus 로고
    • The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH
    • Czajkowsky DM, Iwamoto H, Cover TL, Shao Z. 1999. The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH. Proc Natl Acad SciUSA96:2001-2006. http://dx.doi.org/10.1073/pnas.96.5.2001.
    • (1999) Proc Natl Acad SciUSA , vol.96 , pp. 2001-2006
    • Czajkowsky, D.M.1    Iwamoto, H.2    Cover, T.L.3    Shao, Z.4
  • 18
    • 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
    • Szabo I, Brutsche S, Tombola F, Moschioni M, Satin B, Telford JL, Rappuoli R, Montecucco C, Papini E, Zoratti M. 1999. 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 18:5517-5527. http://dx.doi.org/10.1093/emboj/18.20.5517.
    • (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
  • 19
    • 0033007098 scopus 로고    scopus 로고
    • VacA from Helicobacter pylori: a hexameric chloride channel
    • Iwamoto H, Czajkowsky DM, Cover TL, Szabo G, Shao Z. 1999. VacA from Helicobacter pylori: a hexameric chloride channel. FEBS Lett 450:101-104. http://dx.doi.org/10.1016/S0014-5793(99)00474-3.
    • (1999) FEBS Lett , vol.450 , pp. 101-104
    • Iwamoto, H.1    Czajkowsky, D.M.2    Cover, T.L.3    Szabo, G.4    Shao, Z.5
  • 21
    • 0037561932 scopus 로고    scopus 로고
    • Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin
    • McClain MS, Iwamoto H, Cao P, Vinion-Dubiel AD, Li Y, Szabo G, Shao Z, Cover TL. 2003. Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin. J Biol Chem 278:12101-12108. http://dx.doi.org/10.1074/jbc.M212595200.
    • (2003) J Biol Chem , vol.278 , pp. 12101-12108
    • McClain, M.S.1    Iwamoto, H.2    Cao, P.3    Vinion-Dubiel, A.D.4    Li, Y.5    Szabo, G.6    Shao, Z.7    Cover, T.L.8
  • 22
    • 84960145647 scopus 로고    scopus 로고
    • Helicobacter pylori diversity and gastric cancer risk
    • Cover TL. 2016. Helicobacter pylori diversity and gastric cancer risk. mBio 7:e01869-15. http://dx.doi.org/10.1128/mBio.01869-15.
    • (2016) mBio , vol.7 , pp. e01869-15
    • Cover, T.L.1
  • 24
    • 0029059733 scopus 로고
    • Mosaicism in vacuolating cytotoxin alleles of Helicobacter pylori:association of specific vacA types with cytotoxin production and peptic ulceration
    • Atherton JC, Cao P, Peek RM, Jr, Tummuru MK, Blaser MJ, Cover TL. 1995. Mosaicism in vacuolating cytotoxin alleles of Helicobacter pylori:association of specific vacA types with cytotoxin production and peptic ulceration. J Biol Chem 270:17771-17777.
    • (1995) J Biol Chem , vol.270 , pp. 17771-17777
    • Atherton, J.C.1    Cao, P.2    Peek, R.M.3    Tummuru, M.K.4    Blaser, M.J.5    Cover, T.L.6
  • 25
    • 34548495047 scopus 로고    scopus 로고
    • A new Helicobacter pylori vacuolating cytotoxin determinant, the intermediate region, is associated with gastric cancer
    • Rhead JL, Letley DP, Mohammadi M, Hussein N, Mohagheghi MA, Eshagh Hosseini M, Atherton JC. 2007. A new Helicobacter pylori vacuolating cytotoxin determinant, the intermediate region, is associated with gastric cancer. Gastroenterology 133:926-936. http://dx.doi.org/10.1053/j.gastro.2007.06.056.
    • (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
  • 27
    • 0030809535 scopus 로고    scopus 로고
    • Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating cytotoxin, reveals its pattern of assembly
    • Cover TL, Hanson PI, Heuser JE. 1997. Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating cytotoxin, reveals its pattern of assembly. J Cell Biol 138:759-769. http://dx.doi.org/10.1083/jcb.138.4.759.
    • (1997) J Cell Biol , vol.138 , pp. 759-769
    • Cover, T.L.1    Hanson, P.I.2    Heuser, J.E.3
  • 28
    • 0031928120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of metal replicas of the Helicobacter pylori vacuolating cytotoxin
    • Lanzavecchia S, Bellon PL, Lupetti P, Dallai R, Rappuoli R, Telford JL. 1998. Three-dimensional reconstruction of metal replicas of the Helicobacter pylori vacuolating cytotoxin. J Struct Biol 121:9-18. http://dx.doi .org/10.1006/jsbi.1997.3941.
    • (1998) J Struct Biol , vol.121 , pp. 9-18
    • Lanzavecchia, S.1    Bellon, P.L.2    Lupetti, P.3    Dallai, R.4    Rappuoli, R.5    Telford, J.L.6
  • 29
    • 0036307727 scopus 로고    scopus 로고
    • Multiple oligomeric states of the Helicobacter pylori vacuolating toxin demonstrated by cryoelectron microscopy
    • Adrian M, Cover TL, Dubochet J, Heuser JE. 2002. Multiple oligomeric states of the Helicobacter pylori vacuolating toxin demonstrated by cryoelectron microscopy. J Mol Biol 318:121-133. http://dx.doi.org/10.1016/S0022-2836(02)00047-5.
    • (2002) J Mol Biol , vol.318 , pp. 121-133
    • Adrian, M.1    Cover, T.L.2    Dubochet, J.3    Heuser, J.E.4
  • 30
    • 25144442682 scopus 로고    scopus 로고
    • High-resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryonegative staining electron microscopy
    • El-Bez C, Adrian M, Dubochet J, Cover TL. 2005. High-resolution structural analysis of Helicobacter pylori VacA toxin oligomers by cryonegative staining electron microscopy. J Struct Biol 151:215-228. http://dx.doi.org/10.1016/j.jsb.2005.07.001.
    • (2005) J Struct Biol , vol.151 , pp. 215-228
    • El-Bez, C.1    Adrian, M.2    Dubochet, J.3    Cover, T.L.4
  • 33
    • 46449135449 scopus 로고    scopus 로고
    • Helicobacter pylori VacA subdomain required for intracellular toxin activity and assembly of functional oligomeric complexes
    • Ivie SE, McClain MS, Torres VJ, Algood HM, Lacy DB, Yang R, Blanke SR, Cover TL. 2008. Helicobacter pylori VacA subdomain required for intracellular toxin activity and assembly of functional oligomeric complexes. Infect Immun 76:2843-2851. http://dx.doi.org/10.1128/IAI.01664-07.
    • (2008) Infect Immun , vol.76 , pp. 2843-2851
    • Ivie, S.E.1    McClain, M.S.2    Torres, V.J.3    Algood, H.M.4    Lacy, D.B.5    Yang, R.6    Blanke, S.R.7    Cover, T.L.8
  • 34
    • 0028308711 scopus 로고
    • Divergence of genetic sequences for the vacuolating cytotoxin among Helicobacter pylori strains
    • Cover TL, Tummuru MKR, Cao P, Thompson SA, Blaser MJ. 1994. Divergence of genetic sequences for the vacuolating cytotoxin among Helicobacter pylori strains. J Biol Chem 269:10566-10573.
    • (1994) J Biol Chem , vol.269 , pp. 10566-10573
    • Cover, T.L.1    Tummuru, M.K.R.2    Cao, P.3    Thompson, S.A.4    Blaser, M.J.5
  • 35
    • 0028365481 scopus 로고
    • Genetic analysis of the Helicobacter pylori vacuolating cytotoxin: structural similarities with the IgA protease type of exported protein
    • Schmitt W, Haas R. 1994. Genetic analysis of the Helicobacter pylori vacuolating cytotoxin: structural similarities with the IgA protease type of exported protein. Mol Microbiol 12:307-319. http://dx.doi.org/10.1111/j.1365-2958.1994.tb01019.x.
    • (1994) Mol Microbiol , vol.12 , pp. 307-319
    • Schmitt, W.1    Haas, R.2
  • 37
    • 0034783458 scopus 로고    scopus 로고
    • Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori
    • Fischer W, Buhrdorf R, Gerland E, Haas R. 2001. Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori. Infect Immun 69:6769-6775. http://dx.doi .org/10.1128/IAI.69.11.6769-6775.2001.
    • (2001) Infect Immun , vol.69 , pp. 6769-6775
    • Fischer, W.1    Buhrdorf, R.2    Gerland, E.3    Haas, R.4
  • 38
    • 84902007682 scopus 로고    scopus 로고
    • Analysis of surfaceexposed outer membrane proteins in Helicobacter pylori
    • Voss BJ, Gaddy JA, McDonald WH, Cover TL. 2014. Analysis of surfaceexposed outer membrane proteins in Helicobacter pylori. J Bacteriol 196:2455-2471. http://dx.doi.org/10.1128/JB.01768-14.
    • (2014) J Bacteriol , vol.196 , pp. 2455-2471
    • Voss, B.J.1    Gaddy, J.A.2    McDonald, W.H.3    Cover, T.L.4
  • 39
    • 0036223741 scopus 로고    scopus 로고
    • Functional complementation reveals the importance of intermolecular monomer interactions for Helicobacter pylori VacA vacuolating activity
    • Ye D, Blanke SR. 2002. Functional complementation reveals the importance of intermolecular monomer interactions for Helicobacter pylori VacA vacuolating activity. Mol Microbiol 43:1243-1253. http://dx.doi.org/10.1046/j.1365-2958.2002.02818.x.
    • (2002) Mol Microbiol , vol.43 , pp. 1243-1253
    • Ye, D.1    Blanke, S.R.2
  • 40
    • 0346457086 scopus 로고    scopus 로고
    • Interactions between p-33 and p-55 domains of the Helicobacter pylori vacuolating cytotoxin (VacA)
    • Torres VJ, McClain MS, Cover TL. 2004. Interactions between p-33 and p-55 domains of the Helicobacter pylori vacuolating cytotoxin (VacA). J Biol Chem 279:2324-2331. http://dx.doi.org/10.1074/jbc.M310159200.
    • (2004) J Biol Chem , vol.279 , pp. 2324-2331
    • Torres, V.J.1    McClain, M.S.2    Cover, T.L.3
  • 41
    • 20444426199 scopus 로고    scopus 로고
    • Functional properties of the p33 and p55 domains of the Helicobacter pylori vacuolating cytotoxin
    • Torres VJ, Ivie SE, McClain MS, Cover TL. 2005. Functional properties of the p33 and p55 domains of the Helicobacter pylori vacuolating cytotoxin. J Biol Chem 280:21107-21114. http://dx.doi.org/10.1074/jbc .M501042200.
    • (2005) J Biol Chem , vol.280 , pp. 21107-21114
    • Torres, V.J.1    Ivie, S.E.2    McClain, M.S.3    Cover, T.L.4
  • 45
    • 0033515453 scopus 로고    scopus 로고
    • Identification of the minimal intracellular vacuolating domain of the Helicobacter pylori vacuolating toxin
    • Ye D, Willhite DC, Blanke SR. 1999. Identification of the minimal intracellular vacuolating domain of the Helicobacter pylori vacuolating toxin. J Biol Chem 274:9277-9282. http://dx.doi.org/10.1074/jbc.274.14.9277.
    • (1999) J Biol Chem , vol.274 , pp. 9277-9282
    • Ye, D.1    Willhite, D.C.2    Blanke, S.R.3
  • 48
    • 77955557491 scopus 로고    scopus 로고
    • Both the p33 and p55 subunits of the Helicobacter pylori VacA toxin are targeted to mammalian mitochondria
    • Foo JH, Culvenor JG, Ferrero RL, Kwok T, Lithgow T, Gabriel K. 2010. Both the p33 and p55 subunits of the Helicobacter pylori VacA toxin are targeted to mammalian mitochondria. J Mol Biol 401:792-798. http://dx .doi.org/10.1016/j.jmb.2010.06.065.
    • (2010) J Mol Biol , vol.401 , pp. 792-798
    • Foo, J.H.1    Culvenor, J.G.2    Ferrero, R.L.3    Kwok, T.4    Lithgow, T.5    Gabriel, K.6
  • 49
    • 0033942982 scopus 로고    scopus 로고
    • Mutational analysis of the Helicobacter pylori vacuolating toxin amino terminus: identification of amino acids essential for cellular vacuolation
    • Ye D, Blanke SR. 2000. Mutational analysis of the Helicobacter pylori vacuolating toxin amino terminus: identification of amino acids essential for cellular vacuolation. Infect Immun 68:4354-4357. http://dx.doi.org/10.1128/IAI.68.7.4354-4357.2000.
    • (2000) Infect Immun , vol.68 , pp. 4354-4357
    • Ye, D.1    Blanke, S.R.2
  • 50
    • 0035145404 scopus 로고    scopus 로고
    • Amino-terminal hydrophobic region of Helicobacter pylori vacuolating cytotoxin (VacA) mediates transmembrane protein dimerization
    • McClain MS, Cao P, Cover TL. 2001. Amino-terminal hydrophobic region of Helicobacter pylori vacuolating cytotoxin (VacA) mediates transmembrane protein dimerization. Infect Immun 69:1181-1184. http://dx .doi.org/10.1128/IAI.69.2.1181-1184.2001.
    • (2001) Infect Immun , vol.69 , pp. 1181-1184
    • McClain, M.S.1    Cao, P.2    Cover, T.L.3
  • 51
    • 33750485022 scopus 로고    scopus 로고
    • Random mutagenesis of Helicobacter pylori vacA to identify amino acids essential for vacuolating cytotoxic activity
    • McClain MS, Czajkowsky DM, Torres VJ, Szabo G, Shao Z, Cover TL. 2006. Random mutagenesis of Helicobacter pylori vacA to identify amino acids essential for vacuolating cytotoxic activity. Infect Immun 74:6188-6195. http://dx.doi.org/10.1128/IAI.00915-06.
    • (2006) Infect Immun , vol.74 , pp. 6188-6195
    • McClain, M.S.1    Czajkowsky, D.M.2    Torres, V.J.3    Szabo, G.4    Shao, Z.5    Cover, T.L.6
  • 53
    • 77649327186 scopus 로고    scopus 로고
    • Analysis of a beta-helical region in the p55 domain of Helicobacter pylori vacuolating toxin
    • Ivie SE, McClain MS, Algood HM, Lacy DB, Cover TL. 2010. Analysis of a beta-helical region in the p55 domain of Helicobacter pylori vacuolating toxin. BMC Microbiol 10:60. http://dx.doi.org/10.1186/1471-2180-10-60.
    • (2010) BMC Microbiol , vol.10 , pp. 60
    • Ivie, S.E.1    McClain, M.S.2    Algood, H.M.3    Lacy, D.B.4    Cover, T.L.5
  • 54
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker M, Schuster CC, McDonnell AV, Sorg KA, Finn MC, Berger B, Clark PL. 2006. Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc Natl Acad Sci U S A 103:4918-4923. http://dx.doi.org/10.1073/pnas.0507923103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4918-4923
    • Junker, M.1    Schuster, C.C.2    McDonnell, A.V.3    Sorg, K.A.4    Finn, M.C.5    Berger, B.6    Clark, P.L.7
  • 55
    • 1942501695 scopus 로고    scopus 로고
    • Membrane channel structure of Helicobacter pylori vacuolating toxin: role of multiple GXXXG motifs in cylindrical channels
    • Kim S, Chamberlain AK, Bowie JU. 2004. Membrane channel structure of Helicobacter pylori vacuolating toxin: role of multiple GXXXG motifs in cylindrical channels. Proc Natl Acad Sci U S A 101:5988-5991. http://dx .doi.org/10.1073/pnas.0308694101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5988-5991
    • Kim, S.1    Chamberlain, A.K.2    Bowie, J.U.3
  • 56
    • 84879350365 scopus 로고    scopus 로고
    • In silico investigation and structural characterization of virulent factor and a metallo peptidase present in Helicobacter pylori strain J99
    • Vaidya M, Panchal H. 2012. In silico investigation and structural characterization of virulent factor and a metallo peptidase present in Helicobacter pylori strain J99. Interdiscip Sci 4:302-309. http://dx.doi.org/10.1007/s12539-012-0145-6.
    • (2012) Interdiscip Sci , vol.4 , pp. 302-309
    • Vaidya, M.1    Panchal, H.2
  • 58
    • 84858226117 scopus 로고    scopus 로고
    • Effects of cholesterol on Helicobacter pylori growth and virulence properties in vitro
    • Jimenez-Soto LF, Rohrer S, Jain U, Ertl C, Sewald X, Haas R. 2012. Effects of cholesterol on Helicobacter pylori growth and virulence properties in vitro. Helicobacter 17:133-139. http://dx.doi.org/10.1111/j.1523-5378.2011.00926.x.
    • (2012) Helicobacter , vol.17 , pp. 133-139
    • Jimenez-Soto, L.F.1    Rohrer, S.2    Jain, U.3    Ertl, C.4    Sewald, X.5    Haas, R.6
  • 59
    • 80053460306 scopus 로고    scopus 로고
    • Helicobacter pylori exploits a unique repertoire of type IV secretion system components for pilus assembly at the bacterium-host cell interface
    • Shaffer CL, Gaddy JA, Loh JT, Johnson EM, Hill S, Hennig EE, McClain MS, McDonald WH, Cover TL. 2011. Helicobacter pylori exploits a unique repertoire of type IV secretion system components for pilus assembly at the bacterium-host cell interface. PLoS Pathog 7:e1002237. http://dx .doi.org/10.1371/journal.ppat.1002237.
    • (2011) PLoS Pathog , vol.7
    • Shaffer, C.L.1    Gaddy, J.A.2    Loh, J.T.3    Johnson, E.M.4    Hill, S.5    Hennig, E.E.6    McClain, M.S.7    McDonald, W.H.8    Cover, T.L.9
  • 60
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt TG, Skerra A. 2007. The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat Protoc 2:1528-1535. http://dx.doi.org/10.1038/nprot.2007.209.
    • (2007) Nat Protoc , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 62
    • 0033929821 scopus 로고    scopus 로고
    • Acidactivation of Helicobacter pylori vacuolating cytotoxin (VacA) results in toxin internalization by eukaryotic cells
    • McClain MS, Schraw W, Ricci V, Boquet P, Cover TL. 2000. Acidactivation of Helicobacter pylori vacuolating cytotoxin (VacA) results in toxin internalization by eukaryotic cells. Mol Microbiol 37:433-442. http://dx.doi.org/10.1046/j.1365-2958.2000.02013.x.
    • (2000) Mol Microbiol , vol.37 , pp. 433-442
    • McClain, M.S.1    Schraw, W.2    Ricci, V.3    Boquet, P.4    Cover, T.L.5
  • 63
    • 0026062034 scopus 로고
    • Effect of urease on HeLa cell vacuolation induced by Helicobacter pylori cytotoxin
    • Cover TL, Puryear W, Pérez-Pérez GI, Blaser MJ. 1991. Effect of urease on HeLa cell vacuolation induced by Helicobacter pylori cytotoxin. Infect Immun 59:1264-1270.
    • (1991) Infect Immun , vol.59 , pp. 1264-1270
    • Cover, T.L.1    Puryear, W.2    Pérez-Pérez, G.I.3    Blaser, M.J.4
  • 66
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. http://dx.doi .org/10.1016/S0076-6879(97)76066-X.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 67
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A, Teplyakov A. 1997. MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30:1022-1025. http://dx.doi.org/10.1107/S0021889897006766.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 68
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60:2126-2132. http://dx.doi .org/10.1107/S0907444904019158.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 69
    • 0035158890 scopus 로고    scopus 로고
    • Carboxy-terminal proteolytic processing of Helicobacter pylori vacuolating toxin
    • Nguyen VQ, Caprioli RM, Cover TL. 2001. Carboxy-terminal proteolytic processing of Helicobacter pylori vacuolating toxin. Infect Immun 69:543-546. http://dx.doi.org/10.1128/IAI.69.1.543-546.2001.
    • (2001) Infect Immun , vol.69 , pp. 543-546
    • Nguyen, V.Q.1    Caprioli, R.M.2    Cover, T.L.3
  • 70
    • 33645511453 scopus 로고    scopus 로고
    • Mapping of a domain required for protein-protein interactions and inhibitory activity of a Helicobacter pylori dominant-negative VacA mutant protein
    • Torres VJ, McClain MS, Cover TL. 2006. Mapping of a domain required for protein-protein interactions and inhibitory activity of a Helicobacter pylori dominant-negative VacA mutant protein. Infect Immun 74:2093-2101. http://dx.doi.org/10.1128/IAI.74.4.2093-2101.2006.
    • (2006) Infect Immun , vol.74 , pp. 2093-2101
    • Torres, V.J.1    McClain, M.S.2    Cover, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.