메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Reconstitution of cholesterol-dependent vaginolysin into tethered phospholipid bilayers: Implications for bioanalysis

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; CYTOLYSIN; UNCLASSIFIED DRUG; VAGINOLYSIN;

EID: 84892665272     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0082536     Document Type: Article
Times cited : (25)

References (47)
  • 1
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex
    • doi:10.1016/j.bbamem.2011.07.036. PubMed: 21835159
    • Hotze EM, Tweten RK (2012) Membrane assembly of the cholesterol-dependent cytolysin pore complex. Biochim Biophys Acta 1818: 1028-1038. doi:10.1016/j.bbamem.2011.07.036. PubMed: 21835159.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2
  • 2
    • 0035179919 scopus 로고    scopus 로고
    • Synergistic effects of alpha-toxin and perfringolysin O in Clostridium perfringens-mediated gas gangrene
    • doi: 10.1128/IAI.69.12.7904-7910.2001. PubMed: 11705975
    • Awad MM, Ellemor DM, Boyd RL, Emmins JJ, Rood JI (2001) Synergistic effects of alpha-toxin and perfringolysin O in Clostridium perfringens-mediated gas gangrene. Infect Immun 69: 7904-7910. doi: 10.1128/IAI.69.12.7904-7910.2001. PubMed: 11705975.
    • (2001) Infect Immun , vol.69 , pp. 7904-7910
    • Awad, M.M.1    Ellemor, D.M.2    Boyd, R.L.3    Emmins, J.J.4    Rood, J.I.5
  • 3
    • 48749111836 scopus 로고    scopus 로고
    • The MACPF/CDC family of pore-forming toxins
    • doi:10.1111/j.1462-5822.2008.01191.x. PubMed: 18564372
    • Rosado CJ, Kondos S, Bull TE, Kuiper MJ, Law RHP et al. (2008) The MACPF/CDC family of pore-forming toxins. Cell Microbiol 10: 1765-1774. doi:10.1111/j.1462-5822.2008.01191.x. PubMed: 18564372.
    • (2008) Cell Microbiol , vol.10 , pp. 1765-1774
    • Rosado, C.J.1    Kondos, S.2    Bull, T.E.3    Kuiper, M.J.4    Law, R.H.P.5
  • 4
    • 24744436164 scopus 로고    scopus 로고
    • Intermedilysin is essential for the invasion of hepatoma HepG2 cells by Streptococcus intermedius
    • doi:10.1111/j.1348-0421.2005.tb03647.x. PubMed: 16034212
    • Sukeno A, Nagamune H, Whiley RA, Jafar SI, Aduse-Opoku J et al. (2005) Intermedilysin is essential for the invasion of hepatoma HepG2 cells by Streptococcus intermedius. Microbiol Immunol 49: 681-694. doi:10.1111/j.1348- 0421.2005.tb03647.x. PubMed: 16034212.
    • (2005) Microbiol Immunol , vol.49 , pp. 681-694
    • Sukeno, A.1    Nagamune, H.2    Whiley, R.A.3    Jafar, S.I.4    Aduse-Opoku, J.5
  • 5
    • 84871859276 scopus 로고    scopus 로고
    • Identification and characterization of the first cholesterol-dependent cytolysins from gram-negative bacteria
    • doi: 10.1128/IAI.00927-12. PubMed: 23115036
    • Hotze EM, Le HM, Sieber JR, Bruxvoort C, McInerney MJ et al. (2013) Identification and characterization of the first cholesterol-dependent cytolysins from gram-negative bacteria. Infect Immun 81: 216-225. doi: 10.1128/IAI.00927-12. PubMed: 23115036.
    • (2013) Infect Immun , vol.81 , pp. 216-225
    • Hotze, E.M.1    Le, H.M.2    Sieber, J.R.3    Bruxvoort, C.4    McInerney, M.J.5
  • 6
    • 44349190402 scopus 로고    scopus 로고
    • Functional and phylogenetic characterization of vaginolysin, the human-specific cytolysin from Gardnerella vaginalis
    • doi: 10.1128/JB.01965-07. PubMed: 18390664
    • Gelber SE, Aguilar JL, Lewis KLT, Ratner AJ (2008) Functional and phylogenetic characterization of vaginolysin, the human-specific cytolysin from Gardnerella vaginalis. J Bacteriol 190: 3896-3903. doi: 10.1128/JB.01965-07. PubMed: 18390664.
    • (2008) J Bacteriol , vol.190 , pp. 3896-3903
    • Gelber, S.E.1    Aguilar, J.L.2    Lewis, K.L.T.3    Ratner, A.J.4
  • 7
    • 0026684273 scopus 로고
    • Gardnerella vaginalis: Characteristics, clinical considerations, and controversies
    • PubMed: 1498765
    • Catlin BW (1992) Gardnerella vaginalis: characteristics, clinical considerations, and controversies. Clin Microbiol Rev 5: 213-237. PubMed: 1498765.
    • (1992) Clin Microbiol Rev , vol.5 , pp. 213-237
    • Catlin, B.W.1
  • 8
    • 74049128981 scopus 로고    scopus 로고
    • High vaginal concentrations of Atopobium vaginae and Gardnerella vaginalis in women undergoing preterm labor
    • doi:10.1097/AOG.0b013e3181c391d7. PubMed: 20027045
    • Menard JP, Mazouni C, Salem-Cherif I, Fenollar F, Raoult D et al. (2010) High vaginal concentrations of Atopobium vaginae and Gardnerella vaginalis in women undergoing preterm labor. Obstet Gynecol 115: 134-140. doi:10.1097/AOG.0b013e3181c391d7. PubMed: 20027045.
    • (2010) Obstet Gynecol , vol.115 , pp. 134-140
    • Menard, J.P.1    Mazouni, C.2    Salem-Cherif, I.3    Fenollar, F.4    Raoult, D.5
  • 9
    • 49849099241 scopus 로고    scopus 로고
    • Bacterial vaginosis and HIV acquisition: A meta-analysis of published studies
    • doi:10.1097/QAD.0b013e3283021a37. PubMed: 18614873
    • Atashili J, Poole C, Ndumbe PM, Adimora AA, Smith JS (2008) Bacterial vaginosis and HIV acquisition: a meta-analysis of published studies. AIDS 22: 1493-1501. doi:10.1097/QAD.0b013e3283021a37. PubMed: 18614873.
    • (2008) AIDS , vol.22 , pp. 1493-1501
    • Atashili, J.1    Poole, C.2    Ndumbe, P.M.3    Adimora, A.A.4    Smith, J.S.5
  • 11
    • 84872195010 scopus 로고    scopus 로고
    • Presence of a polymicrobial endometrial biofilm in patients with bacterial vaginosis
    • doi: 10.1371/journal.pone.0053997. PubMed: 23320114
    • Swidsinski A, Verstraelen H, Loening-Baucke V, Swidsinski S, Mendling W et al. (2013) Presence of a polymicrobial endometrial biofilm in patients with bacterial vaginosis. PLOS ONE 8: e53997. doi: 10.1371/journal.pone.0053997. PubMed: 23320114.
    • (2013) PLOS ONE , vol.8
    • Swidsinski, A.1    Verstraelen, H.2    Loening-Baucke, V.3    Swidsinski, S.4    Mendling, W.5
  • 12
    • 84876916642 scopus 로고    scopus 로고
    • Degradation, foraging, and depletion of mucus sialoglycans by the vagina-adapted Actinobacterium Gardnerella vaginalis
    • doi:10.1074/jbc.M113.453654. PubMed: 23479734
    • Lewis WG, Robinson LS, Gilbert NM, Perry JC, Lewis AL (2013) Degradation, foraging, and depletion of mucus sialoglycans by the vagina-adapted Actinobacterium Gardnerella vaginalis. J Biol Chem 288: 12067-12079. doi:10.1074/jbc.M113.453654. PubMed: 23479734.
    • (2013) J Biol Chem , vol.288 , pp. 12067-12079
    • Lewis, W.G.1    Robinson, L.S.2    Gilbert, N.M.3    Perry, J.C.4    Lewis, A.L.5
  • 13
    • 77952553446 scopus 로고    scopus 로고
    • Production and characterization of monoclonal antibodies against vaginolysin: Mapping of a region critical for its cytolytic activity
    • doi:10.1016/j.toxicon.2010.03.007. PubMed: 20298711
    • Zvirbliene A, Pleckaityte M, Lasickiene R, Kucinskaite-Kodze I, Zvirblis G (2010) Production and characterization of monoclonal antibodies against vaginolysin: mapping of a region critical for its cytolytic activity. Toxicon 56: 19-28. doi:10.1016/j.toxicon.2010.03.007. PubMed: 20298711.
    • (2010) Toxicon , vol.56 , pp. 19-28
    • Zvirbliene, A.1    Pleckaityte, M.2    Lasickiene, R.3    Kucinskaite-Kodze, I.4    Zvirblis, G.5
  • 14
    • 84860515168 scopus 로고    scopus 로고
    • Genetic and biochemical diversity of Gardnerella vaginalis strains isolated from women with bacterial vaginosis
    • doi:10.1111/j.1574-695X.2012.00940.x. PubMed: 22309200
    • Pleckaityte M, Janulaitiene M, Lasickiene R, Zvirbliene A (2012) Genetic and biochemical diversity of Gardnerella vaginalis strains isolated from women with bacterial vaginosis. FEMS Immunol Med Microbiol 65: 69-77. doi:10.1111/j.1574-695X.2012.00940.x. PubMed: 22309200.
    • (2012) FEMS Immunol Med Microbiol , vol.65 , pp. 69-77
    • Pleckaityte, M.1    Janulaitiene, M.2    Lasickiene, R.3    Zvirbliene, A.4
  • 16
    • 65349155195 scopus 로고    scopus 로고
    • Antibody-based detection and inhibition of vaginolysin, the Gardnerella vaginalis cytolysin
    • doi:10.1371/journal.pone.0005207. PubMed: 19370149
    • Randis TM, Kulkarni R, Aguilar JL, Ratner AJ (2009) Antibody-based detection and inhibition of vaginolysin, the Gardnerella vaginalis cytolysin. PLOS ONE 4: e5207. doi:10.1371/journal.pone.0005207. PubMed: 19370149.
    • (2009) PLOS ONE , vol.4
    • Randis, T.M.1    Kulkarni, R.2    Aguilar, J.L.3    Ratner, A.J.4
  • 17
    • 0031554429 scopus 로고    scopus 로고
    • A biosensor that uses ion-channel switches
    • doi:10.1038/42432. PubMed: 9177344
    • Cornell BA, Braach-Maksvytis VL, King LG, Osman PD, Raguse B et al. (1997) A biosensor that uses ion-channel switches. Nature 387: 580-583. doi:10.1038/42432. PubMed: 9177344.
    • (1997) Nature , vol.387 , pp. 580-583
    • Cornell, B.A.1    Braach-Maksvytis, V.L.2    King, L.G.3    Osman, P.D.4    Raguse, B.5
  • 18
    • 0030739753 scopus 로고    scopus 로고
    • The design and synthesis of simple molecular tethers for binding biomembranes to a gold surface
    • doi: 10.1016/S0040-4020(97)00698-4
    • Boden N, Bushby RJ, Clarkson S, Evans SD, Knowles PF et al. (1997) The design and synthesis of simple molecular tethers for binding biomembranes to a gold surface. Tetrahedron 53: 10939-10952. doi: 10.1016/S0040-4020(97)00698-4.
    • (1997) Tetrahedron , vol.53 , pp. 10939-10952
    • Boden, N.1    Bushby, R.J.2    Clarkson, S.3    Evans, S.D.4    Knowles, P.F.5
  • 19
    • 84855682218 scopus 로고    scopus 로고
    • Electrochemicalimpedance spectroscopy of tethered bilayer membranes
    • doi:10.1021/la204054g. PubMed: 22126190
    • Valincius G, Meškauskas T, Ivanauskas F (2012) Electrochemicalimpedance spectroscopy of tethered bilayer membranes. Langmuir 28: 977-990. doi:10.1021/la204054g. PubMed: 22126190.
    • (2012) Langmuir , vol.28 , pp. 977-990
    • Valincius, G.1    Meškauskas, T.2    Ivanauskas, F.3
  • 20
    • 62649144191 scopus 로고    scopus 로고
    • Structure of functional Staphylococcus aureus alpha-hemolysin channels in tethered bilayer lipid membranes
    • doi:10.1016/j.bpj.2008.11.020. PubMed: 19217871
    • McGillivray DJ, Valincius G, Heinrich F, Robertson JWF, Vanderah DJ et al. (2009) Structure of functional Staphylococcus aureus alpha-hemolysin channels in tethered bilayer lipid membranes. Biophys J 96: 1547-1553. doi:10.1016/j.bpj.2008.11.020. PubMed: 19217871.
    • (2009) Biophys J , vol.96 , pp. 1547-1553
    • McGillivray, D.J.1    Valincius, G.2    Heinrich, F.3    Robertson, J.W.F.4    Vanderah, D.J.5
  • 21
    • 33745457909 scopus 로고    scopus 로고
    • Enzyme activity to augment the characterization of tethered bilayer membranes
    • doi: 10.1021/jp0616516. PubMed: 16722717
    • Valincius G, McGillivray DJ, Febo-Ayala W, Vanderah DJ, Kasianowicz JJ et al. (2006) Enzyme activity to augment the characterization of tethered bilayer membranes. J Phys Chem B 110: 10213-10216. doi: 10.1021/jp0616516. PubMed: 16722717.
    • (2006) J Phys Chem B , vol.110 , pp. 10213-10216
    • Valincius, G.1    McGillivray, D.J.2    Febo-Ayala, W.3    Vanderah, D.J.4    Kasianowicz, J.J.5
  • 22
    • 80052379414 scopus 로고    scopus 로고
    • Sensing of pathogenic bacteria based on their interaction with supported bilayer membranes studied by impedance spectroscopy and surface plasmon resonance
    • doi:10.1016/j.bios.2011.07.023. PubMed: 21835605
    • Tun TN, Cameron PJ, Jenkins AT (2011) Sensing of pathogenic bacteria based on their interaction with supported bilayer membranes studied by impedance spectroscopy and surface plasmon resonance. Biosens Bioelectron 28: 227-231. doi:10.1016/j.bios.2011.07.023. PubMed: 21835605.
    • (2011) Biosens Bioelectron , vol.28 , pp. 227-231
    • Tun, T.N.1    Cameron, P.J.2    Jenkins, A.T.3
  • 23
    • 77958052877 scopus 로고    scopus 로고
    • An electrochemical impedance study of the effect of pathogenic bacterial toxins on tethered bilayer lipid membrane
    • doi:10.1016/j.elecom. 2010.07.034
    • Tun TN, Jenkins AT (2010) An electrochemical impedance study of the effect of pathogenic bacterial toxins on tethered bilayer lipid membrane. Electrochem Commun 12: 1411-1415. doi:10.1016/j.elecom. 2010.07.034.
    • (2010) Electrochem Commun , vol.12 , pp. 1411-1415
    • Tun, T.N.1    Jenkins, A.T.2
  • 24
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent tations
    • Menestrina G (1986) Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent tations. J Membr Biol 70: 177-190.
    • (1986) J Membr Biol , vol.70 , pp. 177-190
    • Menestrina, G.1
  • 25
    • 16544370492 scopus 로고    scopus 로고
    • Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin
    • doi:10.1038/nsmb862. PubMed: 15543155
    • Giddings KS, Zhao J, Sims PJ, Tweten RK (2004) Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin. Nat Struct Mol Biol 11: 1173-1178. doi:10.1038/nsmb862. PubMed: 15543155.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1173-1178
    • Giddings, K.S.1    Zhao, J.2    Sims, P.J.3    Tweten, R.K.4
  • 26
    • 79957978193 scopus 로고    scopus 로고
    • Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8 alpha and C9
    • doi:10.1074/jbc.M111.237446. PubMed: 21507937
    • Wickham SE, Hotze EM, Farrand AJ, Polekhina G, Nero TL et al. (2011) Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8 alpha and C9. J Biol Chem 286: 20952-20962. doi:10.1074/jbc.M111.237446. PubMed: 21507937.
    • (2011) J Biol Chem , vol.286 , pp. 20952-20962
    • Wickham, S.E.1    Hotze, E.M.2    Farrand, A.J.3    Polekhina, G.4    Nero, T.L.5
  • 27
    • 0036521875 scopus 로고    scopus 로고
    • CD59 blocks not only the insertion of C9 into MAC but inhibits ion channel formation by homologous C5b-8 as well as C5b-9
    • doi:10.1113/jphysiol.2001.013381. PubMed: 11882685
    • Farkas I, Baranyi L, Ishikawa Y, Okada N, Bohata C et al. (2002) CD59 blocks not only the insertion of C9 into MAC but inhibits ion channel formation by homologous C5b-8 as well as C5b-9. J Physiol 539: 537-545. doi:10.1113/jphysiol.2001.013381. PubMed: 11882685.
    • (2002) J Physiol , vol.539 , pp. 537-545
    • Farkas, I.1    Baranyi, L.2    Ishikawa, Y.3    Okada, N.4    Bohata, C.5
  • 28
    • 85127548795 scopus 로고    scopus 로고
    • Molecular-scale structural and functional characterization of sparsely tethered bilayer lipid membranes
    • doi:10.1116/1.2709308. PubMed: 20408633
    • McGillivray DJ, Valincius G, Vanderah DJ, Febo-Ayala W, Woodward TJ et al. (2007) Molecular-scale structural and functional characterization of sparsely tethered bilayer lipid membranes. Biointerphases 2: 21-32. doi:10.1116/1.2709308. PubMed: 20408633.
    • (2007) Biointerphases , vol.2 , pp. 21-32
    • McGillivray, D.J.1    Valincius, G.2    Vanderah, D.J.3    Febo-Ayala, W.4    Woodward, T.J.5
  • 29
    • 84875773674 scopus 로고    scopus 로고
    • Modification of tethered bilayers by phospholipid exchange with vesicles
    • doi:10.1021/la304613a. PubMed: 23445262
    • Budvytyte R, Mickevicius M, Vanderah DJ, Heinrich F, Valincius G (2013) Modification of tethered bilayers by phospholipid exchange with vesicles. Langmuir 29: 4320-4327. doi:10.1021/la304613a. PubMed: 23445262.
    • (2013) Langmuir , vol.29 , pp. 4320-4327
    • Budvytyte, R.1    Mickevicius, M.2    Vanderah, D.J.3    Heinrich, F.4    Valincius, G.5
  • 30
    • 0032477653 scopus 로고    scopus 로고
    • Tethered lipid bilayer membranes: Formation and ionic reservoir characterization
    • doi:10.1021/la9711239
    • Raguse B, Braach-Maksvytis V, Cornell BA, King LG, Osman PD et al. (1998) Tethered lipid bilayer membranes: formation and ionic reservoir characterization. Langmuir 14: 648-659. doi:10.1021/la9711239.
    • (1998) Langmuir , vol.14 , pp. 648-659
    • Raguse, B.1    Braach-Maksvytis, V.2    Cornell, B.A.3    King, L.G.4    Osman, P.D.5
  • 31
    • 77951022973 scopus 로고    scopus 로고
    • Size-dependent neurotoxicity of beta-amyloid oligomers
    • doi:10.1016/j.abb.2010.02.001. PubMed: 20153288
    • Cizas P, Budvytyte R, Morkuniene R, Moldovan R, Broccio M et al. (2010) Size-dependent neurotoxicity of beta-amyloid oligomers. Arch Biochem Biophys 496: 84-92. doi:10.1016/j.abb.2010.02.001. PubMed: 20153288.
    • (2010) Arch Biochem Biophys , vol.496 , pp. 84-92
    • Cizas, P.1    Budvytyte, R.2    Morkuniene, R.3    Moldovan, R.4    Broccio, M.5
  • 32
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • doi:10.1073/pnas.0911581107. PubMed: 20145114
    • Farrand AJ, LaChapelle S, Hotze EM, Johnson AE, Tweten RK (2010) Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci U S A 107: 4341-4346. doi:10.1073/pnas. 0911581107. PubMed: 20145114.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4341-4346
    • Farrand, A.J.1    LaChapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 33
    • 33845735655 scopus 로고    scopus 로고
    • Mapping of B cell epitopes in measles virus nucleocapsid protein
    • doi:10.1007/s00705-006-0837-5. PubMed: 16944047
    • Zvirbliene A, Kucinskaite I, Sezaite I, Samuel D, Sasnauskas K (2007) Mapping of B cell epitopes in measles virus nucleocapsid protein. Arch Virol 152: 25-39. doi:10.1007/s00705-006-0837-5. PubMed: 16944047.
    • (2007) Arch Virol , vol.152 , pp. 25-39
    • Zvirbliene, A.1    Kucinskaite, I.2    Sezaite, I.3    Samuel, D.4    Sasnauskas, K.5
  • 34
    • 84864771243 scopus 로고    scopus 로고
    • Combined electrochemistry and surface-enhanced infrared absorption spectroscopy of gramicidin A incorporated into tethered bilayer lipid membranes
    • doi:10.1002/anie.201203214. PubMed: 22865570
    • Kozuch J, Steinem C, Hildebrandt P, Millo D (2012) Combined electrochemistry and surface-enhanced infrared absorption spectroscopy of gramicidin A incorporated into tethered bilayer lipid membranes. Angew Chem Int Ed Engl 51: 8114-8117. doi:10.1002/anie.201203214. PubMed: 22865570.
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 8114-8117
    • Kozuch, J.1    Steinem, C.2    Hildebrandt, P.3    Millo, D.4
  • 35
    • 0031194564 scopus 로고    scopus 로고
    • Designed protein pores as components for biosensors
    • doi:10.1016/S1074-5521(97)90321-5. PubMed: 9263637
    • Braha O, Walker B, Cheley S, Kasianowicz JJ, Song LZ et al. (1997) Designed protein pores as components for biosensors. Chem Biol 4: 497-505. doi:10.1016/S1074-5521(97)90321-5. PubMed: 9263637.
    • (1997) Chem Biol , vol.4 , pp. 497-505
    • Braha, O.1    Walker, B.2    Cheley, S.3    Kasianowicz, J.J.4    Song, L.Z.5
  • 36
    • 26644461678 scopus 로고    scopus 로고
    • Anthrax biosensor, protective antigen ion channel asymmetric blockade
    • doi:10.1074/jbc.M507928200. PubMed: 16087661
    • Halverson KM, Panchal RG, Nguyen TL, Gussio R, Little SF et al. (2005) Anthrax biosensor, protective antigen ion channel asymmetric blockade. J Biol Chem 280: 34056-34062. doi:10.1074/jbc.M507928200. PubMed: 16087661.
    • (2005) J Biol Chem , vol.280 , pp. 34056-34062
    • Halverson, K.M.1    Panchal, R.G.2    Nguyen, T.L.3    Gussio, R.4    Little, S.F.5
  • 37
    • 0034874625 scopus 로고    scopus 로고
    • Tethered-bilayer lipid membranes as a support for membrane-active peptides
    • doi:10.1042/BST0290613. PubMed: 11498038
    • Cornell BA, Krishna G, Osman PD, Pace RD, Wieczorek L (2001) Tethered-bilayer lipid membranes as a support for membrane-active peptides. Biochem Soc Trans 29: 613-617. doi:10.1042/BST0290613. PubMed: 11498038.
    • (2001) Biochem Soc Trans , vol.29 , pp. 613-617
    • Cornell, B.A.1    Krishna, G.2    Osman, P.D.3    Pace, R.D.4    Wieczorek, L.5
  • 38
    • 0035822853 scopus 로고    scopus 로고
    • Tethered bilayer membranes containing ionic reservoirs: The interfacial capacitance
    • doi:10.1021/la001480a
    • Krishna G, Schulte J, Cornell BA, Pace R, Wieczorek L et al. (2001) Tethered bilayer membranes containing ionic reservoirs: the interfacial capacitance. Langmuir 17: 4858-4866. doi:10.1021/la001480a.
    • (2001) Langmuir , vol.17 , pp. 4858-4866
    • Krishna, G.1    Schulte, J.2    Cornell, B.A.3    Pace, R.4    Wieczorek, L.5
  • 39
    • 58149277415 scopus 로고    scopus 로고
    • Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: Implications for cell toxicity
    • doi:10.1529/biophysj.108.130997. PubMed: 18515395
    • Valincius G, Heinrich F, Budvytyte R, Vanderah DJ, McGillivray DJ et al. (2008) Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: implications for cell toxicity. Biophys J 95: 4845-4861. doi:10.1529/biophysj.108.130997. PubMed: 18515395.
    • (2008) Biophys J , vol.95 , pp. 4845-4861
    • Valincius, G.1    Heinrich, F.2    Budvytyte, R.3    Vanderah, D.J.4    McGillivray, D.J.5
  • 40
    • 3543016107 scopus 로고    scopus 로고
    • Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment
    • doi:10.1038/nsmb793. PubMed: 15235590
    • Ramachandran R, Tweten RK, Johnson AE (2004) Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment. Nat Struct Mol Biol 11: 697-705. doi:10.1038/nsmb793. PubMed: 15235590.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 697-705
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 41
    • 79952615728 scopus 로고    scopus 로고
    • Probing protein-membrane interactions using solid supported membranese
    • doi:10.1021/la103200k
    • Junghans A, Champagne C, Cayot P, Loupiac C, Koper I (2011) Probing protein-membrane interactions using solid supported membranese. Langmuir 27: 2709-2716. doi:10.1021/la103200k.
    • (2011) Langmuir , vol.27 , pp. 2709-2716
    • Junghans, A.1    Champagne, C.2    Cayot, P.3    Loupiac, C.4    Koper, I.5
  • 42
    • 36349022766 scopus 로고    scopus 로고
    • Performance of a pneumolysin enzyme-linked immunosorbent assay for diagnosis of pneumococcal infections
    • doi:10.1128/JCM.01030-07. PubMed: 17728474
    • del Mar García-Suárez M, Cima-Cabal MD, Villaverde R, Espinosa E, Falguera M et al. (2007) Performance of a pneumolysin enzyme-linked immunosorbent assay for diagnosis of pneumococcal infections. J Clin Microbiol 45: 3549-3554. doi:10.1128/JCM.01030-07. PubMed: 17728474.
    • (2007) J Clin Microbiol , vol.45 , pp. 3549-3554
    • Del Mar García-Suárez, M.1    Cima-Cabal, M.D.2    Villaverde, R.3    Espinosa, E.4    Falguera, M.5
  • 43
    • 84892646637 scopus 로고    scopus 로고
    • Available: Accessed 22 July 2013
    • Weisstein E (2013) WolframMathWorld. Available: http://mathworld.wolfram. com/OblateSpheroid.html. Accessed 22 July 2013
    • (2013)
    • Weisstein, E.1
  • 44
    • 67649819389 scopus 로고    scopus 로고
    • Intermedilysin-receptor interactions during assembly of the pore complex: Assembly intermediates increase host cell susceptibility to complement-mediated lysis
    • doi:10.1074/jbc.M900772200. PubMed: 19293153
    • LaChapelle S, Tweten RK, Hotze EM (2009) Intermedilysin-receptor interactions during assembly of the pore complex: assembly intermediates increase host cell susceptibility to complement-mediated lysis. J Biol Chem 284: 12719-12726. doi:10.1074/jbc.M900772200. PubMed: 19293153.
    • (2009) J Biol Chem , vol.284 , pp. 12719-12726
    • LaChapelle, S.1    Tweten, R.K.2    Hotze, E.M.3
  • 45
    • 61449223579 scopus 로고    scopus 로고
    • Regenerable tethered bilayer lipid membrane arrays for multiplexed label-free analysis of lipid-protein interactions on poly(dimethylsiloxane) microchips using SPR imaging
    • doi: 10.1021/ac8023137. PubMed: 19178341
    • Taylor JD, Linman MJ, Wilkop T, Cheng Q (2009) Regenerable tethered bilayer lipid membrane arrays for multiplexed label-free analysis of lipid-protein interactions on poly(dimethylsiloxane) microchips using SPR imaging. Anal Chem 81: 1146-1153. doi: 10.1021/ac8023137. PubMed: 19178341.
    • (2009) Anal Chem , vol.81 , pp. 1146-1153
    • Taylor, J.D.1    Linman, M.J.2    Wilkop, T.3    Cheng, Q.4
  • 46
    • 0037021522 scopus 로고    scopus 로고
    • Surface-bound lipid vesicles encapsulating redox species for amperometric biosensing of pore-forming bacterial toxins
    • doi:10.1021/ja027897f. PubMed: 12452699
    • Xu DK, Cheng Q (2002) Surface-bound lipid vesicles encapsulating redox species for amperometric biosensing of pore-forming bacterial toxins. J Am Chem Soc 124: 14314-14315. doi:10.1021/ja027897f. PubMed: 12452699.
    • (2002) J Am Chem Soc , vol.124 , pp. 14314-14315
    • Xu, D.K.1    Cheng, Q.2
  • 47
    • 44649138020 scopus 로고    scopus 로고
    • Electrochemical characterization of pore formation by bacterial protein toxins on hybrid supported membranes
    • doi:10.1021/la704027c. PubMed: 18402473
    • Wilkop T, Xu DK, Cheng Q (2008) Electrochemical characterization of pore formation by bacterial protein toxins on hybrid supported membranes. Langmuir 24: 5615-5621. doi:10.1021/la704027c. PubMed: 18402473.
    • (2008) Langmuir , vol.24 , pp. 5615-5621
    • Wilkop, T.1    Xu, D.K.2    Cheng, Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.