메뉴 건너뛰기




Volumn 25, Issue 5, 2008, Pages 388-400

Effect of dipole potential of lipid bilayers on properties of ion channels formed by cyclic lipodepsipeptide syringomycin E

Author keywords

[No Author keywords available]

Indexed keywords

PSEUDOMONAS SYRINGAE;

EID: 57049162494     PISSN: 02334755     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (77)
  • 1
    • 77957067380 scopus 로고
    • Electrostatic potentials at membrane-solution interfaces
    • P
    • McLaughlin S. Electrostatic potentials at membrane-solution interfaces // Curr. Topics Membr. Transport. 1977. V. 9. P. 71-144.
    • (1977) Curr. Topics Membr. Transport , vol.9 , pp. 71-144
    • McLaughlin, S.1
  • 2
    • 0027177939 scopus 로고    scopus 로고
    • Franklin J.C., Cafiso D.S. Internal electrostatic potentials in bilayers: measuring and controlling dipole potentials in lipid vesicles // Biophys. J. 1993. V. 65. P. 289-299.
    • Franklin J.C., Cafiso D.S. Internal electrostatic potentials in bilayers: measuring and controlling dipole potentials in lipid vesicles // Biophys. J. 1993. V. 65. P. 289-299.
  • 3
    • 0027982642 scopus 로고    scopus 로고
    • Brockman H. Dipole potential of lipid membranes // Chem. Phys. Lipids. 1994. V. 73. P. 57-79.
    • Brockman H. Dipole potential of lipid membranes // Chem. Phys. Lipids. 1994. V. 73. P. 57-79.
  • 5
    • 57049189878 scopus 로고    scopus 로고
    • Sokolov V.S., Mirsky V.M. Electrostatic potentials of bilayer lipid membranes: basic research and analytical applications // Ultrathin Electrochemical Chemo- and Biosensors: Technology and Performance/Ed. Mirsky V.M. Heidelberg: Springer-Verlag, 2004. P. 255-291.
    • Sokolov V.S., Mirsky V.M. Electrostatic potentials of bilayer lipid membranes: basic research and analytical applications // Ultrathin Electrochemical Chemo- and Biosensors: Technology and Performance/Ed. Mirsky V.M. Heidelberg: Springer-Verlag, 2004. P. 255-291.
  • 6
    • 0026635481 scopus 로고    scopus 로고
    • Gawrisch K., Ruston D., Zimmerberg J., Parsegian V.A., Rand R.P., Fuller N. Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces // Biophys. J. 1992. V. 61. P. 1213-1223.
    • Gawrisch K., Ruston D., Zimmerberg J., Parsegian V.A., Rand R.P., Fuller N. Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces // Biophys. J. 1992. V. 61. P. 1213-1223.
  • 7
    • 0022670331 scopus 로고    scopus 로고
    • Flewelling R.F., Hubbell W.L. The membrane dipole potential in a total membrane potential model. Applications to hydrophobic ion interactions with membranes // Biophys. J. 1986. V. 49. P. 541-552.
    • Flewelling R.F., Hubbell W.L. The membrane dipole potential in a total membrane potential model. Applications to hydrophobic ion interactions with membranes // Biophys. J. 1986. V. 49. P. 541-552.
  • 8
    • 0000800213 scopus 로고    scopus 로고
    • Brock W., Stark G., Jordan P.C. A laser-temperature-jump method for the study of the rate of transfer of hydrophobic ions and carriers across the interface of thin lipid membranes // Biophys. Chem. 1981. V. 13. P. 329-348.
    • Brock W., Stark G., Jordan P.C. A laser-temperature-jump method for the study of the rate of transfer of hydrophobic ions and carriers across the interface of thin lipid membranes // Biophys. Chem. 1981. V. 13. P. 329-348.
  • 9
    • 0036671109 scopus 로고    scopus 로고
    • Peterson U., Mannock D.A., Lewis R.N., Pohl P., McElhaney R.N., Pohl E.E. Origin of membrane dipole potential: contribution of the phospholipid fatty acid chains // Chem. Phys. Lipids. 2002. V. 117. P. 19-27.
    • Peterson U., Mannock D.A., Lewis R.N., Pohl P., McElhaney R.N., Pohl E.E. Origin of membrane dipole potential: contribution of the phospholipid fatty acid chains // Chem. Phys. Lipids. 2002. V. 117. P. 19-27.
  • 10
    • 0342933118 scopus 로고    scopus 로고
    • Pickar A.D., Benz R. Transport of oppositely charged lipophilic probe ions in lipid bilayer membranes having various structures // J. Membr. Biol. 1978. V. 44. P. 353-376.
    • Pickar A.D., Benz R. Transport of oppositely charged lipophilic probe ions in lipid bilayer membranes having various structures // J. Membr. Biol. 1978. V. 44. P. 353-376.
  • 11
    • 4444348709 scopus 로고    scopus 로고
    • Brockman H.L., Momsen MM., Brown R.E., He L., Chun J., Byun H.S., Bittman R. The 4,5-double bond of ceramide regulates its dipole potential, elastic properties, and packing behavior // Biophys. J. 2004. V. 87. P. 1722-1731.
    • Brockman H.L., Momsen MM., Brown R.E., He L., Chun J., Byun H.S., Bittman R. The 4,5-double bond of ceramide regulates its dipole potential, elastic properties, and packing behavior // Biophys. J. 2004. V. 87. P. 1722-1731.
  • 12
    • 0017161652 scopus 로고    scopus 로고
    • Andersen O.S., Finkelstein A., Katz I., Cass A. Effect of phloretin on the permeability of thin lipid membranes // J. Gen. Physiol. 1976. V. 67. P. 749-771.
    • Andersen O.S., Finkelstein A., Katz I., Cass A. Effect of phloretin on the permeability of thin lipid membranes // J. Gen. Physiol. 1976. V. 67. P. 749-771.
  • 13
    • 0017357683 scopus 로고    scopus 로고
    • Melnik E., Latorre R., Hall J.E., Tosteson D.C. Phloretin-induced changes in ion transport across lipid bilayer membranes // J. Gen. Physiol. 1977. V. 69. P. 243-257.
    • Melnik E., Latorre R., Hall J.E., Tosteson D.C. Phloretin-induced changes in ion transport across lipid bilayer membranes // J. Gen. Physiol. 1977. V. 69. P. 243-257.
  • 14
    • 0017875057 scopus 로고    scopus 로고
    • Wang C.C., Brimer L.J. Lipid-dependent and phloretin-induced modifications of dipicrylamine adsorption by bilayer membranes // Nature. 1978. V. 272. P. 268-270.
    • Wang C.C., Brimer L.J. Lipid-dependent and phloretin-induced modifications of dipicrylamine adsorption by bilayer membranes // Nature. 1978. V. 272. P. 268-270.
  • 15
    • 0020584454 scopus 로고    scopus 로고
    • Reyes J., Motais R., Latorre R. Phloretin and phloretin analogs: mode of action in planar lipid bilayers // J. Membr. Biol. 1983. V. 72. P. 93-103.
    • Reyes J., Motais R., Latorre R. Phloretin and phloretin analogs: mode of action in planar lipid bilayers // J. Membr. Biol. 1983. V. 72. P. 93-103.
  • 16
    • 57049153627 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 17
    • 0031910472 scopus 로고    scopus 로고
    • Cseh R., Benz R. The adsorption of phloretin to lipid monolayers and bilayers cannot be explained by langmuir adsorption isotherms alone // Biophys. J. 1998. V. 74. P. 1399-1408.
    • Cseh R., Benz R. The adsorption of phloretin to lipid monolayers and bilayers cannot be explained by langmuir adsorption isotherms alone // Biophys. J. 1998. V. 74. P. 1399-1408.
  • 18
    • 0032839450 scopus 로고    scopus 로고
    • Cseh R., Benz K. Interaction of phloretin with lipid monolayers: relationship between structural changes and dipole potential change // Biophys. J. 1999. V. 77. p. 1477-1488.
    • Cseh R., Benz K. Interaction of phloretin with lipid monolayers: relationship between structural changes and dipole potential change // Biophys. J. 1999. V. 77. p. 1477-1488.
  • 19
    • 57049153100 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 20
    • 0032974758 scopus 로고    scopus 로고
    • Shapovalov V.L., Kotova E.A., Rokitskaya T.I., Antimenko Y.N. Effect of gramicidin A on the dipole potential of phospholipid membranes // Biophys. J. 1999. V. 77. P. 299-305.
    • Shapovalov V.L., Kotova E.A., Rokitskaya T.I., Antimenko Y.N. Effect of gramicidin A on the dipole potential of phospholipid membranes // Biophys. J. 1999. V. 77. P. 299-305.
  • 21
    • 0030070198 scopus 로고    scopus 로고
    • Malkov D.Y., Sokolov V.S. Fluorescent styryl dyes of the RH series affect a potential drop on the membrane/solution boundary // Biochim. et biophys. acta. 1996. V. 1278. P. 197-204.
    • Malkov D.Y., Sokolov V.S. Fluorescent styryl dyes of the RH series affect a potential drop on the membrane/solution boundary // Biochim. et biophys. acta. 1996. V. 1278. P. 197-204.
  • 22
    • 57049133128 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 23
    • 0031958516 scopus 로고    scopus 로고
    • Cladera J., O'Shea P. Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide // Biophys. J. 1998. V. 74. P. 2434-2442.
    • Cladera J., O'Shea P. Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide // Biophys. J. 1998. V. 74. P. 2434-2442.
  • 24
    • 0024453540 scopus 로고    scopus 로고
    • Sargent D.F., Bean J.W., Schwyzer R. Reversible binding of substance P to artificial lipid membranes studied by capacitance minimization techniques // Biophys. Chem. 1989. V. 34. P. 103-114.
    • Sargent D.F., Bean J.W., Schwyzer R. Reversible binding of substance P to artificial lipid membranes studied by capacitance minimization techniques // Biophys. Chem. 1989. V. 34. P. 103-114.
  • 25
    • 0037108271 scopus 로고    scopus 로고
    • Yano Y., Matsuzaki K. Membrane insertion and dissociation processes of a model transmembrane helix // Biochemistry. 2002. V. 41. P. 12407-12413.
    • Yano Y., Matsuzaki K. Membrane insertion and dissociation processes of a model transmembrane helix // Biochemistry. 2002. V. 41. P. 12407-12413.
  • 26
    • 33845929560 scopus 로고    scopus 로고
    • Buzon V., Cladera J. Effect of cholesterol on the interaction of the HIV GP41 fusion peptide with model membranes. Importance of the membrane dipole potential // Biochemistry. 2006. V. 45. P. 15768-15775.
    • Buzon V., Cladera J. Effect of cholesterol on the interaction of the HIV GP41 fusion peptide with model membranes. Importance of the membrane dipole potential // Biochemistry. 2006. V. 45. P. 15768-15775.
  • 27
    • 0025285274 scopus 로고    scopus 로고
    • Dalbey R.E. Positively charged residues are important determinants of membrane protein topology // Trends Biochem. Sci. 1990. V. 15. P. 253-257.
    • Dalbey R.E. Positively charged residues are important determinants of membrane protein topology // Trends Biochem. Sci. 1990. V. 15. P. 253-257.
  • 28
    • 0032587171 scopus 로고    scopus 로고
    • Maggio B. Modulation of phospholipase A2 by electrostatic fields and dipole potential of glycosphingolipids in monolayers // J. Lipid Res. 1999. V. 40. P. 930-939.
    • Maggio B. Modulation of phospholipase A2 by electrostatic fields and dipole potential of glycosphingolipids in monolayers // J. Lipid Res. 1999. V. 40. P. 930-939.
  • 29
    • 0035914384 scopus 로고    scopus 로고
    • Asawakarn T., Cladera J., O'Shea P. Effects of the membrane dipole potential on the interaction of saquinavir with phospholipid membranes and plasma membrane receptors of Caco-2 cells // J. Biol. Chem. 2001. V. 276. P. 38457-38463.
    • Asawakarn T., Cladera J., O'Shea P. Effects of the membrane dipole potential on the interaction of saquinavir with phospholipid membranes and plasma membrane receptors of Caco-2 cells // J. Biol. Chem. 2001. V. 276. P. 38457-38463.
  • 30
    • 0036189651 scopus 로고    scopus 로고
    • Severina I.I., Muntyan M.S., Lewis K., Skulachev V.P. Transfer of cationic antibacterial agents berberine, palmatine, and benzalkonium through bimolecular planar phospholipid film and Staphylococcus aureus membrane // IUBMB Life. 2001. V. 52. P. 321-324.
    • Severina I.I., Muntyan M.S., Lewis K., Skulachev V.P. Transfer of cationic antibacterial agents berberine, palmatine, and benzalkonium through bimolecular planar phospholipid film and Staphylococcus aureus membrane // IUBMB Life. 2001. V. 52. P. 321-324.
  • 31
    • 0037408151 scopus 로고    scopus 로고
    • Cladera J., O'Shea P., Hadgraft J., Valenta C. Influence of molecular dipoles on human skin permeability: Use of 6-ketocholestanol to enhance the transdermal delivery of bacitracin // J. Pharm. Sci. 2003. V. 92. P. 1018-1027.
    • Cladera J., O'Shea P., Hadgraft J., Valenta C. Influence of molecular dipoles on human skin permeability: Use of 6-ketocholestanol to enhance the transdermal delivery of bacitracin // J. Pharm. Sci. 2003. V. 92. P. 1018-1027.
  • 32
    • 3042663176 scopus 로고    scopus 로고
    • Alakoskela J.M., Soderlund T., Holopainen J.M., Kinnunen P.K. Dipole potential and head-group spacing are determinants for the membrane partitioning of pregnanolone // Mol. Pharmacol. 2004. V. 66. P. 161-168.
    • Alakoskela J.M., Soderlund T., Holopainen J.M., Kinnunen P.K. Dipole potential and head-group spacing are determinants for the membrane partitioning of pregnanolone // Mol. Pharmacol. 2004. V. 66. P. 161-168.
  • 33
    • 0016164242 scopus 로고    scopus 로고
    • Hladky S.B. The energy barriers to ion transport by nonactin across thin lipid membranes // Biochim. et biophys. acta. 1974. V. 352. P. 71-85.
    • Hladky S.B. The energy barriers to ion transport by nonactin across thin lipid membranes // Biochim. et biophys. acta. 1974. V. 352. P. 71-85.
  • 34
    • 0018938695 scopus 로고    scopus 로고
    • MrLaughlin S.C.J., Dilger L.P. Transport of protons across membranes by weak acids // Physiol. Rev. 1980. V. 60. P. 825-863.
    • MrLaughlin S.C.J., Dilger L.P. Transport of protons across membranes by weak acids // Physiol. Rev. 1980. V. 60. P. 825-863.
  • 35
    • 0035830617 scopus 로고    scopus 로고
    • + in phospholipid vesicles // Biochim. et biophys. acta. 2001. V. 1510. P. 258-269.
    • + in phospholipid vesicles // Biochim. et biophys. acta. 2001. V. 1510. P. 258-269.
  • 36
    • 0023110334 scopus 로고    scopus 로고
    • Jordan P.C. How pore mouth charge distributions alter the permeability of transmembrane ionic channels // Biophys. J. 1987. V. 51. P. 297-311.
    • Jordan P.C. How pore mouth charge distributions alter the permeability of transmembrane ionic channels // Biophys. J. 1987. V. 51. P. 297-311.
  • 37
    • 0031058750 scopus 로고    scopus 로고
    • 2 + influx // Biochem J. 1997. V. 32. P. 691-698.
    • 2 + influx // Biochem J. 1997. V. 32. P. 691-698.
  • 38
    • 29344465372 scopus 로고    scopus 로고
    • 2+-transporting ATPase reconstituted into diacylphosphatidylcholine vesicles: effects of bilayer physical parameters // Biophys. Chem. 2006. V. 119. P. 69-77.
    • 2+-transporting ATPase reconstituted into diacylphosphatidylcholine vesicles: effects of bilayer physical parameters // Biophys. Chem. 2006. V. 119. P. 69-77.
  • 39
    • 0030851433 scopus 로고    scopus 로고
    • Rokitskaya T.I., Antonenko Y.N., Kotova E.A. Effect of the dipole potential of a bilayer lipid membrane on gramicidin channel dissociation kinetics // Biophys. J. 1997. V. 73. P. 850-854.
    • Rokitskaya T.I., Antonenko Y.N., Kotova E.A. Effect of the dipole potential of a bilayer lipid membrane on gramicidin channel dissociation kinetics // Biophys. J. 1997. V. 73. P. 850-854.
  • 40
    • 0031769568 scopus 로고    scopus 로고
    • Busath D.D., Thulin C.D., Hendershot R.W., Phillips L.R., Maughan P., Cole C.D., Bingham N.C., Morrison S., Baird L.C., Hendershot R.J., Gotten M., Cross T.A. Noncontact dipole effects on channel permeation. I. Experiments with (5F-indole)Trp13 gramicidin A channels // Biophys. J. 1998. V. 75. P. 2830-2844.
    • Busath D.D., Thulin C.D., Hendershot R.W., Phillips L.R., Maughan P., Cole C.D., Bingham N.C., Morrison S., Baird L.C., Hendershot R.J., Gotten M., Cross T.A. Noncontact dipole effects on channel permeation. I. Experiments with (5F-indole)Trp13 gramicidin A channels // Biophys. J. 1998. V. 75. P. 2830-2844.
  • 41
    • 0345254912 scopus 로고    scopus 로고
    • Hwang T.C., Koeppe R.E. 2nd, Andersen O.S. Genistein can modulate channel function by a phosphorylation-independent mechanism: importance of hydrophobic mismatch and bilayer mechanics // Biochemistry. 2003. V. 42. P. 13646-13658.
    • Hwang T.C., Koeppe R.E. 2nd, Andersen O.S. Genistein can modulate channel function by a phosphorylation-independent mechanism: importance of hydrophobic mismatch and bilayer mechanics // Biochemistry. 2003. V. 42. P. 13646-13658.
  • 42
    • 0037452689 scopus 로고    scopus 로고
    • Duffin R.L., Garrett M.P., Flake K.B., Durrant J.D., Busath D.D. Modulation of lipid bilayer interfacial dipole potential by phloretin, RH 421, and 6-ketocholestanol as probed by gramicidin channel conductance // Langmuir. 2003. V. 19. P. 1439-1442.
    • Duffin R.L., Garrett M.P., Flake K.B., Durrant J.D., Busath D.D. Modulation of lipid bilayer interfacial dipole potential by phloretin, RH 421, and 6-ketocholestanol as probed by gramicidin channel conductance // Langmuir. 2003. V. 19. P. 1439-1442.
  • 43
    • 33749610849 scopus 로고    scopus 로고
    • Luchian T., Mereuta L. Phlorizin- and 6-ketocholestanol-mediated antagonistic modulation of alamethicin activity in phospholipid planar membranes // Langmuir. 2006. V. 22. P. 8452-8457.
    • Luchian T., Mereuta L. Phlorizin- and 6-ketocholestanol-mediated antagonistic modulation of alamethicin activity in phospholipid planar membranes // Langmuir. 2006. V. 22. P. 8452-8457.
  • 44
    • 0019286990 scopus 로고    scopus 로고
    • Latorre R., Donovan J.J. Modulation of alamethicin-induced conductance by membrane composition // Acta Physiol. Scand. Suppl. 1980. V. 481. P. 37-45.
    • Latorre R., Donovan J.J. Modulation of alamethicin-induced conductance by membrane composition // Acta Physiol. Scand. Suppl. 1980. V. 481. P. 37-45.
  • 45
    • 0019458461 scopus 로고    scopus 로고
    • Latorre R., Alvarez O. Voltage-dependent channels in planar lipid bilayer membranes // Physiol. Rev. 1981. V. 61. P. 77-150.
    • Latorre R., Alvarez O. Voltage-dependent channels in planar lipid bilayer membranes // Physiol. Rev. 1981. V. 61. P. 77-150.
  • 46
    • 0030030826 scopus 로고    scopus 로고
    • Feigin A.M., Takemoto J.Y., Wangspa R., Teeter J.H., Brand J.C. Properties of voltage-gated ion channels formed by syringomycin E in planar lipid bilayers // J. Membr. Biol. 1996. V. 149. P. 41-47.
    • Feigin A.M., Takemoto J.Y., Wangspa R., Teeter J.H., Brand J.C. Properties of voltage-gated ion channels formed by syringomycin E in planar lipid bilayers // J. Membr. Biol. 1996. V. 149. P. 41-47.
  • 47
    • 57049151499 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 48
    • 0031806923 scopus 로고    scopus 로고
    • Kaulin Y.A., Schagina L.V., Bezrukov S.M., Malev V.V., Feigin A.M., Takemoto J.Y., Teeter J.H., Brand J.G. Cluster organization of ion channels formed by the antibiotic syringomycin E in bilayer lipid membranes // Biophys. J. 1998. V. 74. P. 2918-2925.
    • Kaulin Y.A., Schagina L.V., Bezrukov S.M., Malev V.V., Feigin A.M., Takemoto J.Y., Teeter J.H., Brand J.G. Cluster organization of ion channels formed by the antibiotic syringomycin E in bilayer lipid membranes // Biophys. J. 1998. V. 74. P. 2918-2925.
  • 49
    • 26844570655 scopus 로고    scopus 로고
    • Ostroumova O.S., Malev V.V., Kaulin Yu.A., Gurnev Ph.A., Takemoto J.Y., Schagina L.V. Voltage-dependent synchronization of gating of syringomycin E ion channels // FEBS Letters. 2005. V. 579. P. 5675-5679.
    • Ostroumova O.S., Malev V.V., Kaulin Yu.A., Gurnev Ph.A., Takemoto J.Y., Schagina L.V. Voltage-dependent synchronization of gating of syringomycin E ion channels // FEBS Letters. 2005. V. 579. P. 5675-5679.
  • 50
    • 57049091845 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 51
    • 0036217618 scopus 로고    scopus 로고
    • Malev V.V., Schagina L.V., Gurnev P.A., Takemoto J. Y., Nestorovich E.M., Bezrukov S.M. Syringomycin E channel: a lipidic pore stabilized by lipopeptide? // Biophys. J. 2002. V. 82. P. 1985-1994.
    • Malev V.V., Schagina L.V., Gurnev P.A., Takemoto J. Y., Nestorovich E.M., Bezrukov S.M. Syringomycin E channel: a lipidic pore stabilized by lipopeptide? // Biophys. J. 2002. V. 82. P. 1985-1994.
  • 52
    • 33847185579 scopus 로고    scopus 로고
    • Ostroumova O.S., Gurnev P.A., Schagina L.V., Bezrukov S.M. Asymmetry of syringomycin E channel studied by polymer partitioning // FEBS Lett. 2007. V. 581. P. 04-808.
    • Ostroumova O.S., Gurnev P.A., Schagina L.V., Bezrukov S.M. Asymmetry of syringomycin E channel studied by polymer partitioning // FEBS Lett. 2007. V. 581. P. 04-808.
  • 53
    • 57049156723 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 54
    • 57049169367 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 55
    • 0029808503 scopus 로고    scopus 로고
    • Sorensen K.N., Kim K.H., Takemoto J.Y. In vitro antifungal and fungicidal activities and erythrocyte toxicities of cyclic lipodepsinonapeptides produced by Pseudomonas syringae pv. syringae // Antimicrob. Agents Chemother. 1996. V. 40. P. 2710-2713.
    • Sorensen K.N., Kim K.H., Takemoto J.Y. In vitro antifungal and fungicidal activities and erythrocyte toxicities of cyclic lipodepsinonapeptides produced by Pseudomonas syringae pv. syringae // Antimicrob. Agents Chemother. 1996. V. 40. P. 2710-2713.
  • 56
    • 0342684500 scopus 로고    scopus 로고
    • Lavermicocca P., Iacobellis N.S., Simmaco M., Graniti A. Biological properties and spectrum of activity of Pseudomonas syringae pv. syringae toxins // Physiol. Mol. Plant Pathol. 1997. V. 50. P. 129-140.
    • Lavermicocca P., Iacobellis N.S., Simmaco M., Graniti A. Biological properties and spectrum of activity of Pseudomonas syringae pv. syringae toxins // Physiol. Mol. Plant Pathol. 1997. V. 50. P. 129-140.
  • 57
    • 0035369368 scopus 로고    scopus 로고
    • Walsh U.F., Morrissey J.P., O'Gara F. Pseudomonas for biocontrol of phytopathogens: from functional genomics to commercial exploitation // Curr. Opin. Biotechnol. 2001. V. 12. P. 289-295.
    • Walsh U.F., Morrissey J.P., O'Gara F. Pseudomonas for biocontrol of phytopathogens: from functional genomics to commercial exploitation // Curr. Opin. Biotechnol. 2001. V. 12. P. 289-295.
  • 58
    • 0036890244 scopus 로고    scopus 로고
    • Buber E., Stindl A., Acan N.L., Kocagoz T., Zacher R. Antimycobacterial activity of lipodepsipeptides produced by Pseudomonas svringae pv. svringae B359 // Nat. Prod. Lett. 2002. V. 16. P. 419-423.
    • Buber E., Stindl A., Acan N.L., Kocagoz T., Zacher R. Antimycobacterial activity of lipodepsipeptides produced by Pseudomonas svringae pv. svringae B359 // Nat. Prod. Lett. 2002. V. 16. P. 419-423.
  • 59
    • 57049143348 scopus 로고    scopus 로고
    • Takemoto J.Y.. Brand J.G., Kaulin Y.A., Malev V.V., Schagina L.V., Blasko K. The syringomycins: lipodepsipeptide pore formers from plant bacterium Pseudomonas syringae/Eds. Menestrina G., Dalla Serra M., Lazarovici P. Pore forming peptides and protein toxins. London: Taylor&Francis. 2003. P. 260-271.
    • Takemoto J.Y.. Brand J.G., Kaulin Y.A., Malev V.V., Schagina L.V., Blasko K. The syringomycins: lipodepsipeptide pore formers from plant bacterium Pseudomonas syringae/Eds. Menestrina G., Dalla Serra M., Lazarovici P. Pore forming peptides and protein toxins. London: Taylor&Francis. 2003. P. 260-271.
  • 60
    • 57049127833 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 61
    • 57049142811 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 62
    • 33646460601 scopus 로고    scopus 로고
    • Bessonov A.N., Schagina L.V., Takemoto J.Y., Gurnev P.A., Kuznetsova I.M., Turoverov K.K., Malev V.V. Actin and amphiphilic polymers influence on channel formation by syringomycin E in lipid bilayers // Eur. Biophys. J. 2006. V. 35. P. 382-392.
    • Bessonov A.N., Schagina L.V., Takemoto J.Y., Gurnev P.A., Kuznetsova I.M., Turoverov K.K., Malev V.V. Actin and amphiphilic polymers influence on channel formation by syringomycin E in lipid bilayers // Eur. Biophys. J. 2006. V. 35. P. 382-392.
  • 63
    • 0032516731 scopus 로고    scopus 로고
    • Blasko K., Schagina L.V., Agner G., Kaulin Y.A., Takemoto J.Y. Membrane sterol composition modulates the pore forming activity of syringomycin E in human red blood cells // Biochim. et biophys. acta. 1998. V. 1373. P. 163-169.
    • Blasko K., Schagina L.V., Agner G., Kaulin Y.A., Takemoto J.Y. Membrane sterol composition modulates the pore forming activity of syringomycin E in human red blood cells // Biochim. et biophys. acta. 1998. V. 1373. P. 163-169.
  • 64
    • 28844467560 scopus 로고    scopus 로고
    • Kaulin Yu.A., Takemoto J.Y., Schagina L.V., Ostroumova O.S., Wangspa R., Teeter J.H., Brand J.G. Sphingolipids influence the sensitivity of lipid bilayers to fungicide, syringomycin E // J. Bioenerg. Biomembr. 2005. V. 37. P. 339-348.
    • Kaulin Yu.A., Takemoto J.Y., Schagina L.V., Ostroumova O.S., Wangspa R., Teeter J.H., Brand J.G. Sphingolipids influence the sensitivity of lipid bilayers to fungicide, syringomycin E // J. Bioenerg. Biomembr. 2005. V. 37. P. 339-348.
  • 65
    • 34547300030 scopus 로고    scopus 로고
    • Ostroumova O.S., Kaulin Y.A., Gurnev Ph.A., Schagina L.V. Effect of agents modifying the membrane dipole potential on properties of syringomycin E channels // Langmuir. 2007. V. 23. P. 6889-6892.
    • Ostroumova O.S., Kaulin Y.A., Gurnev Ph.A., Schagina L.V. Effect of agents modifying the membrane dipole potential on properties of syringomycin E channels // Langmuir. 2007. V. 23. P. 6889-6892.
  • 66
    • 42249096650 scopus 로고    scopus 로고
    • Ostroumova O.S., Malev V.V., Bessonov A.N., Takemoto J.Y., Schagina L.V. Altering the activity of syringomycin E via the membrane dipole potential // Langmuir. 2008. V. 24. P. 2987-2991.
    • Ostroumova O.S., Malev V.V., Bessonov A.N., Takemoto J.Y., Schagina L.V. Altering the activity of syringomycin E via the membrane dipole potential // Langmuir. 2008. V. 24. P. 2987-2991.
  • 67
    • 0015459562 scopus 로고    scopus 로고
    • Montall M., Mueller P. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties // Proc. Natl. Acad. Sci. USA. 1972. V. 69. P. 3561-3566.
    • Montall M., Mueller P. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties // Proc. Natl. Acad. Sci. USA. 1972. V. 69. P. 3561-3566.
  • 68
    • 0033832671 scopus 로고    scopus 로고
    • Cseh R., Hetzer M., Wolf K., Kraus J., Bringmann G., Benz R. Interaction of phloretin with membranes: on the mode of action of phloretin at the water-lipid interface // Eur. Biophys. J. 2000. V. 29. P. 172-183.
    • Cseh R., Hetzer M., Wolf K., Kraus J., Bringmann G., Benz R. Interaction of phloretin with membranes: on the mode of action of phloretin at the water-lipid interface // Eur. Biophys. J. 2000. V. 29. P. 172-183.
  • 69
    • 0043172554 scopus 로고    scopus 로고
    • Schagina L.V., Gurnev Ph.A., Takemoto J.Y., Malev V.V. Effective gating charge of ion channels induced by toxin syringomycin E in lipid bilayers // Bioelectrochemistry. 2003. V. 60. P. 21-27.
    • Schagina L.V., Gurnev Ph.A., Takemoto J.Y., Malev V.V. Effective gating charge of ion channels induced by toxin syringomycin E in lipid bilayers // Bioelectrochemistry. 2003. V. 60. P. 21-27.
  • 70
    • 13844253232 scopus 로고    scopus 로고
    • +-ATPase molecular activity // Am. J. Physiol. Regul. Integr. Comp. Physiol. 2005. V. 288. P. R663-R670.
    • +-ATPase molecular activity // Am. J. Physiol. Regul. Integr. Comp. Physiol. 2005. V. 288. P. R663-R670.
  • 71
    • 9544239640 scopus 로고    scopus 로고
    • Lesslauer W., Richter J., Lauger P. Some electrical properties of bimolecular phosphatidyl inositol membranes // Nature. 1967. V. 213. P. 1224-1226.
    • Lesslauer W., Richter J., Lauger P. Some electrical properties of bimolecular phosphatidyl inositol membranes // Nature. 1967. V. 213. P. 1224-1226.
  • 72
    • 0019795013 scopus 로고    scopus 로고
    • Finkelstein A., Andersen O.S. The gramicidin A channel: a review of its permeability characteristics with special reference to the single-file aspect of transport // J. Membr. Biol. 1981. V. 59. P. 155-171.
    • Finkelstein A., Andersen O.S. The gramicidin A channel: a review of its permeability characteristics with special reference to the single-file aspect of transport // J. Membr. Biol. 1981. V. 59. P. 155-171.
  • 73
    • 0022919787 scopus 로고    scopus 로고
    • Menestrina G., Voges K.P., Jung G., Boheim G. Voltage-dependent channel formation by rods of helical polypeptides // J. Membr. Biol. 1986. V. 93. P. 111-132.
    • Menestrina G., Voges K.P., Jung G., Boheim G. Voltage-dependent channel formation by rods of helical polypeptides // J. Membr. Biol. 1986. V. 93. P. 111-132.
  • 74
    • 0027400112 scopus 로고    scopus 로고
    • Bezrukov S.M., Vodyanoy I. Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states // Biophys. J. 1993. V. 64. P. 16-25.
    • Bezrukov S.M., Vodyanoy I. Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states // Biophys. J. 1993. V. 64. P. 16-25.
  • 75
    • 0020630499 scopus 로고    scopus 로고
    • Jordan P.C. Electrostatic modeling of ion pores. II. Effects attributable to the membrane dipole potential // Biophys. J. 1983. V. 41. P. 189-195.
    • Jordan P.C. Electrostatic modeling of ion pores. II. Effects attributable to the membrane dipole potential // Biophys. J. 1983. V. 41. P. 189-195.
  • 76
    • 57049104798 scopus 로고    scopus 로고
    • Russian source
    • Russian source


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.