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Volumn 73, Issue 2, 1997, Pages 770-778

Intrinsic rectification of ion flux in alamethicin channels: Studies with an alamethicin dimer

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN;

EID: 0030851379     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78109-8     Document Type: Article
Times cited : (50)

References (41)
  • 1
    • 0030024628 scopus 로고    scopus 로고
    • Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling
    • Barranger-Mathys, M., and D. S. Cafiso. 1996. Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling. Biochemistry. 35:498-505.
    • (1996) Biochemistry , vol.35 , pp. 498-505
    • Barranger-Mathys, M.1    Cafiso, D.S.2
  • 3
    • 0028347833 scopus 로고
    • Brownian dynamics study of a multiply occupied cation channel: Application to understanding permeation in potassium channels
    • Bek, S., and E. Jakobsson. 1994. Brownian dynamics study of a multiply occupied cation channel: application to understanding permeation in potassium channels. Biophys. J. 66:1028-1038.
    • (1994) Biophys. J. , vol.66 , pp. 1028-1038
    • Bek, S.1    Jakobsson, E.2
  • 4
    • 0031022167 scopus 로고    scopus 로고
    • Simulation studies of alamethicin bilayer interactions
    • Biggin, P. C., J. Breed, H. S. Son, and M. S. P. Sansom. 1997. Simulation studies of alamethicin bilayer interactions. Biophys. J. 72:627-636.
    • (1997) Biophys. J. , vol.72 , pp. 627-636
    • Biggin, P.C.1    Breed, J.2    Son, H.S.3    Sansom, M.S.P.4
  • 5
    • 0020697109 scopus 로고
    • Alamethicin pore formation: Voltage-dependent flip-flop of α-helix dipoles
    • Boheim, G., W. Hanke, and G. Jung. 1983. Alamethicin pore formation: voltage-dependent flip-flop of α-helix dipoles. Biophys. Struct. Mech. 9:181-191.
    • (1983) Biophys. Struct. Mech. , vol.9 , pp. 181-191
    • Boheim, G.1    Hanke, W.2    Jung, G.3
  • 7
    • 0029863372 scopus 로고    scopus 로고
    • Molecular dynamics simulations of water within models of ion channels
    • Breed, J., R. Sankararamakrishnan, I. D. Kerr, and M. S. P. Sansom. 1996. Molecular dynamics simulations of water within models of ion channels. Biophys. J. 70:1643-1661.
    • (1996) Biophys. J. , vol.70 , pp. 1643-1661
    • Breed, J.1    Sankararamakrishnan, R.2    Kerr, I.D.3    Sansom, M.S.P.4
  • 8
    • 0028238803 scopus 로고
    • Alamethicin channels modelled by simulated annealing and molecular dynamics
    • Breed, J., and M. S. P. Sansom. 1994. Alamethicin channels modelled by simulated annealing and molecular dynamics. Biochem. Soc. Trans. 22:157S.
    • (1994) Biochem. Soc. Trans. , vol.22
    • Breed, J.1    Sansom, M.S.P.2
  • 9
    • 0028226051 scopus 로고
    • Alamethicin: A peptide model for voltage gating and protein-membrane interactions
    • Cafiso, D. S. 1994. Alamethicin: a peptide model for voltage gating and protein-membrane interactions. Annu. Rev. Biophys. Biomol. Struct. 23:141-165.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 10
    • 0000836734 scopus 로고
    • PNP theory fits current-voltage (IV) relations of a synthetic channel in 7 solutions
    • Chen, D., P. Kienker, J. D. Lear, and R. S. Eisenberg. 1995. PNP theory fits current-voltage (IV) relations of a synthetic channel in 7 solutions. Biophys. J. 68:A370.
    • (1995) Biophys. J. , vol.68
    • Chen, D.1    Kienker, P.2    Lear, J.D.3    Eisenberg, R.S.4
  • 12
    • 0026124585 scopus 로고
    • Electrostatics and diffusion of molecules in solution: Simulations with the University of Houston Brownian dynamics program
    • Davis, M. E., J. D. Madura, B. A. Luty, and J. A. McCammon. 1991. Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian dynamics program. Comput. Phys. Comm. 62:187-197.
    • (1991) Comput. Phys. Comm. , vol.62 , pp. 187-197
    • Davis, M.E.1    Madura, J.D.2    Luty, B.A.3    McCammon, J.A.4
  • 13
    • 0015760624 scopus 로고
    • The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes
    • Eisenberg, M., J. Hall, and C. A. Mead. 1973. The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes. J. Membr. Biol. 14:143-176.
    • (1973) J. Membr. Biol. , vol.14 , pp. 143-176
    • Eisenberg, M.1    Hall, J.2    Mead, C.A.3
  • 14
    • 0343453490 scopus 로고
    • Ion Transport via Alamethicin Channels
    • B. A. Callingham, editor. Macmillan, New York
    • Gordon, L. G. M. 1973. Ion Transport via Alamethicin Channels. In Drugs and Transport Processes. B. A. Callingham, editor. Macmillan, New York.
    • (1973) Drugs and Transport Processes
    • Gordon, L.G.M.1
  • 15
    • 0015513556 scopus 로고
    • The unit conductance channel of alamethicin
    • Gordon, L. G. M., and D. A. Haydon. 1972. The unit conductance channel of alamethicin. Biochim. Biophys. Acta. 255:1014-1018.
    • (1972) Biochim. Biophys. Acta , vol.255 , pp. 1014-1018
    • Gordon, L.G.M.1    Haydon, D.A.2
  • 16
    • 0026663131 scopus 로고
    • Quantitation of physical-chemical properties of the aqueous phase inside the PhoE ionic channel
    • Gutman, M., Y. Tsfadia, A. Masad, and E. Nachliel. 1992. Quantitation of physical-chemical properties of the aqueous phase inside the PhoE ionic channel. Biochim. Biophys. Acta. 1109:141-148.
    • (1992) Biochim. Biophys. Acta , vol.1109 , pp. 141-148
    • Gutman, M.1    Tsfadia, Y.2    Masad, A.3    Nachliel, E.4
  • 19
    • 0028070549 scopus 로고
    • Parallel helix bundles and ion channels: Molecular modelling via simulated annealing and restrained molecular dynamics
    • Kerr, I. D., R. Sankararamakrishnan, O. S. Smart, and M. S. P. Sansom. 1994. Parallel helix bundles and ion channels: molecular modelling via simulated annealing and restrained molecular dynamics. Biophys. J. 67:1501-1515.
    • (1994) Biophys. J. , vol.67 , pp. 1501-1515
    • Kerr, I.D.1    Sankararamakrishnan, R.2    Smart, O.S.3    Sansom, M.S.P.4
  • 20
    • 0028278173 scopus 로고
    • A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel
    • Kienker, P. K., W. F. Degrado, and J. D. Lear. 1994. A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel. Proc. Natl. Acad. Sci. USA. 91:4859-4863.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4859-4863
    • Kienker, P.K.1    Degrado, W.F.2    Lear, J.D.3
  • 22
    • 0019458461 scopus 로고
    • Voltage-dependent channels in planar lipid membranes
    • Latorre, R., and O. Alvarez. 1981. Voltage-dependent channels in planar lipid membranes. Physiol. Rev. 77-150.
    • (1981) Physiol. Rev. , pp. 77-150
    • Latorre, R.1    Alvarez, O.2
  • 23
    • 0022102083 scopus 로고
    • Strong electrolyte continuum theory solution for equilibrium profiles, diffusion limitation, and conductance in charged ion channels
    • Levitt, D. G. 1985. Strong electrolyte continuum theory solution for equilibrium profiles, diffusion limitation, and conductance in charged ion channels. Biophys. J. 48:19-31.
    • (1985) Biophys. J. , vol.48 , pp. 19-31
    • Levitt, D.G.1
  • 24
    • 0022522698 scopus 로고
    • Interpretation of biological ion channel flux data: Reaction rate versus continuum theory
    • Levitt, D. G. 1986. Interpretation of biological ion channel flux data: reaction rate versus continuum theory. Annu. Rev. Biophys. Biophys. Chem. 15:29-57.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 29-57
    • Levitt, D.G.1
  • 25
    • 0026011790 scopus 로고
    • General continuum theory for multiion channel. I. Theory
    • Levitt, D. G. 1991a. General continuum theory for multiion channel. I. Theory. Biophys. J. 59:271-277.
    • (1991) Biophys. J. , vol.59 , pp. 271-277
    • Levitt, D.G.1
  • 26
    • 0026078627 scopus 로고
    • General continuum theory for multiion channel. II. Application to acetylcholine channel
    • Levitt, D. G. 1991b. General continuum theory for multiion channel. II. Application to acetylcholine channel. Biophys. J. 59:278-288.
    • (1991) Biophys. J. , vol.59 , pp. 278-288
    • Levitt, D.G.1
  • 27
    • 0028828192 scopus 로고
    • Molecular dynamics of alamethicin transmembrane channels from open-channel current noise analysis
    • Mak, D. D., and W. W. Webb. 1995a. Molecular dynamics of alamethicin transmembrane channels from open-channel current noise analysis. Biophys. J. 69:2337-2349.
    • (1995) Biophys. J. , vol.69 , pp. 2337-2349
    • Mak, D.D.1    Webb, W.W.2
  • 28
    • 0028860483 scopus 로고
    • Two classes of alamethicin transmembrane channels: Molecular models from single channel properties
    • Mak, D. D., and W. W. Webb. 1995b. Two classes of alamethicin transmembrane channels: molecular models from single channel properties. Biophys. J. 69:2323-2336.
    • (1995) Biophys. J. , vol.69 , pp. 2323-2336
    • Mak, D.D.1    Webb, W.W.2
  • 29
    • 0029913429 scopus 로고    scopus 로고
    • Ion channel stabilization of synthetic alamethicin analogs by rings of inter-helix H-bonds
    • Molle, G., J. Y. Dugast, G. Spach, and H. Duclohier. 1996. Ion channel stabilization of synthetic alamethicin analogs by rings of inter-helix H-bonds. Biophys. J. 70:1669-1675.
    • (1996) Biophys. J. , vol.70 , pp. 1669-1675
    • Molle, G.1    Dugast, J.Y.2    Spach, G.3    Duclohier, H.4
  • 31
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols-model ion channels
    • Sansom, M. S. P. 1993a. Alamethicin and related peptaibols-model ion channels. Eur. Biophys. J. 22:105-124.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 105-124
    • Sansom, M.S.P.1
  • 32
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols
    • Sansom, M. S. P. 1993b. Structure and function of channel-forming peptaibols. Q. Rev. Biophys. 26:365-421.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 365-421
    • Sansom, M.S.P.1
  • 34
    • 0027200325 scopus 로고
    • The permeation properties of small organic cations in gramicidin channels
    • Seoh, S., and D. Busath. 1993. The permeation properties of small organic cations in gramicidin channels. Biophys. J. 64:1017-1028.
    • (1993) Biophys. J. , vol.64 , pp. 1017-1028
    • Seoh, S.1    Busath, D.2
  • 36
    • 0025897469 scopus 로고
    • "Reversed" alamethicin conductance in lipid bilayers
    • Taylor, R. J., and R. de Levie. 1991. "Reversed" alamethicin conductance in lipid bilayers. Biophys. J. 59:873-879.
    • (1991) Biophys. J. , vol.59 , pp. 873-879
    • Taylor, R.J.1    De Levie, R.2
  • 37
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. 1995. Acetylcholine receptor channel imaged in the open state. Nature. 373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 38
    • 0020586620 scopus 로고
    • Alamethicin-induced current-voltage curve asymmetry in lipid bilayers
    • Vodyanoy, I., J. E. Hall, and T. M. Balasubramanian. 1983. Alamethicin-induced current-voltage curve asymmetry in lipid bilayers. Biophys. J. 42:71-82.
    • (1983) Biophys. J. , vol.42 , pp. 71-82
    • Vodyanoy, I.1    Hall, J.E.2    Balasubramanian, T.M.3
  • 39
    • 0028223474 scopus 로고
    • Alamethicin-pyromellitate: An ion-activated channel-forming peptide
    • Woolley, G. A., R. M. Epand, I. D. Kerr, M. S. P. Sansom, and B. A. Wallace. 1994. Alamethicin-pyromellitate: an ion-activated channel-forming peptide. Biochemistry. 33:6850-6858.
    • (1994) Biochemistry , vol.33 , pp. 6850-6858
    • Woolley, G.A.1    Epand, R.M.2    Kerr, I.D.3    Sansom, M.S.P.4    Wallace, B.A.5
  • 40
    • 0026754487 scopus 로고
    • Model ion channels: Gramicidin and alamethicin
    • Woolley, G. A., and B. A. Wallace. 1992. Model ion channels: gramicidin and alamethicin. J. Membr. Biol. 129:109-136.
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 41
    • 0029971826 scopus 로고    scopus 로고
    • Engineering stabilized ion channels: Covalent dimers of alamethicin
    • You, S., S. Peng, L. Lien, J. Breed, M. S. P. Sansom, and G. A. Woolley. 1996. Engineering stabilized ion channels: covalent dimers of alamethicin. Biochemistry. 35:6225-6232.
    • (1996) Biochemistry , vol.35 , pp. 6225-6232
    • You, S.1    Peng, S.2    Lien, L.3    Breed, J.4    Sansom, M.S.P.5    Woolley, G.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.