메뉴 건너뛰기




Volumn 85, Issue 1, 2003, Pages 267-273

Ion channels of alamethicin dimer N-terminally linked by disulfide bond

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; DIMER; ION CHANNEL;

EID: 0037974360     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74472-5     Document Type: Article
Times cited : (38)

References (28)
  • 1
    • 0036280431 scopus 로고    scopus 로고
    • Modifications of alamethicin ion-channels by substitution of Glu7 for Gln7
    • Asami, K., T. Okazaki, Y. Nagai, and Y. Nagaoka. 2002. Modifications of alamethicin ion-channels by substitution of Glu7 for Gln7. Biophys. J.83:219-228.
    • (2002) Biophys. J. , vol.83 , pp. 219-228
    • Asami, K.1    Okazaki, T.2    Nagai, Y.3    Nagaoka, Y.4
  • 2
    • 0017869782 scopus 로고
    • Analysis of the multi-pore system of alamethicin in a lipid membrane. I. Voltage-jump current-relaxation measurements
    • Boheim, G., and H. A. Kolb. 1978. Analysis of the multi-pore system of alamethicin in a lipid membrane. I. Voltage-jump current-relaxation measurements. J. Membr. Biol. 38:99-150.
    • (1978) J. Membr. Biol. , vol.38 , pp. 99-150
    • Boheim, G.1    Kolb, H.A.2
  • 3
    • 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. Sruct. 23:141-165.
    • (1994) Annu. Rev. Biophys. Biomol. Sruct. , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 4
    • 0032774824 scopus 로고    scopus 로고
    • C-terminally shortened alamethicin on templates: Influence of the linkers on conductances
    • Duclohier, H., K. Kociolek, M. Stasiak, M. T. Leplawy, and G. R. Marshall. 1999. C-terminally shortened alamethicin on templates: influence of the linkers on conductances. Biochim. Biophys. Acta. 1420:14-22.
    • (1999) Biochim. Biophys. Acta , vol.1420 , pp. 14-22
    • Duclohier, H.1    Kociolek, K.2    Stasiak, M.3    Leplawy, M.T.4    Marshall, G.R.5
  • 5
    • 0024788164 scopus 로고
    • The influence of the trichozianin C-terminal residues on the ion channel conductance in lipid bilayers
    • Duclohier, H., G. Mole, and G. Spach. 1989. The influence of the trichozianin C-terminal residues on the ion channel conductance in lipid bilayers. Biochim. Biophys. Acta. 987:133-136.
    • (1989) Biochim. Biophys. Acta , vol.987 , pp. 133-136
    • Duclohier, H.1    Mole, G.2    Spach, G.3
  • 6
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • Duclohier, H., and H. Wrólewski. 2001. Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J. Membr. Biol. 184:1-12.
    • (2001) J. Membr. Biol. , vol.184 , pp. 1-12
    • Duclohier, H.1    Wrólewski, H.2
  • 7
    • 0015760624 scopus 로고
    • The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes
    • Eisenberg, M., J. E. 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.E.2    Mead, C.A.3
  • 8
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution
    • Fox, R. O., Jr., and F. M. Richards. 1982. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution. Nature. 300:325-330.
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox R.O., Jr.1    Richards, F.M.2
  • 9
    • 0035852013 scopus 로고    scopus 로고
    • Alamethicin-leucine zipper hybrid peptide: A prototype for the design of artificial receptors and ion channels
    • Futaki, S., M. Fukuda, M. Omote, K. Yamauchi, T. Yagami, M. Niwa, and Y. Sugiura. 2001. Alamethicin-leucine zipper hybrid peptide: a prototype for the design of artificial receptors and ion channels. J. Am. Chem. Soc. 123:12127-12134.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12127-12134
    • Futaki, S.1    Fukuda, M.2    Omote, M.3    Yamauchi, K.4    Yagami, T.5    Niwa, M.6    Sugiura, Y.7
  • 10
    • 0030656494 scopus 로고    scopus 로고
    • Structure-function relationships in helix-bundle channels probed via total chemical synthesis of alamethicin dimers: Effects of a Gln7 to Asn Mutation
    • Jaikaran, D. C. J., P. C. Biggin, H. Wenschuh, M. S. P. Sansom, and G. A. Woolley. 1997. Structure-function relationships in helix-bundle channels probed via total chemical synthesis of alamethicin dimers: Effects of a Gln7 to Asn Mutation. Biochemistry. 36:13873-13881.
    • (1997) Biochemistry , vol.36 , pp. 13873-13881
    • Jaikaran, D.C.J.1    Biggin, P.C.2    Wenschuh, H.3    Sansom, M.S.P.4    Woolley, G.A.5
  • 11
    • 0019323459 scopus 로고
    • The lowest conductance state of the alamethicin pore
    • Hanke, W., and G. Boheim. 1980. The lowest conductance state of the alamethicin pore. Biochim. Biophys. Acta. 596:456-462.
    • (1980) Biochim. Biophys. Acta , vol.596 , pp. 456-462
    • Hanke, W.1    Boheim, G.2
  • 13
    • 0028278173 scopus 로고
    • A Helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel
    • Kienker, P. K., W. G. 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.G.2    Lear, J.D.3
  • 15
    • 0030959188 scopus 로고    scopus 로고
    • Ion channels of hypelcins, antibiotic peptides, formed in planar bilayer lipid membranes
    • Koide, N., K. Asami, and T. Fujita. 1997. Ion channels of hypelcins, antibiotic peptides, formed in planar bilayer lipid membranes. Biochim. Biophys. Acta. 1326:47-53.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 47-53
    • Koide, N.1    Asami, K.2    Fujita, T.3
  • 16
    • 0019458461 scopus 로고
    • Voltage-dependent channels in planar lipid bilayer membranes
    • Latorre, R., and O. Alvarez. 1981. Voltage-dependent channels in planar lipid bilayer membranes. Physiol. Rev. 61:77-150.
    • (1981) Physiol. Rev. , vol.61 , pp. 77-150
    • Latorre, R.1    Alvarez, O.2
  • 17
    • 0015984471 scopus 로고
    • Synthesis of [2-p-Fluorophenylalanine]oxytocin and its desamino analogue using the S-acetamidomethyl protecting group
    • Marbach, P., and J. Rudinger. 1974. Synthesis of [2-p-Fluorophenylalanine]oxytocin and its desamino analogue using the S-acetamidomethyl protecting group. Helvetica Chimica Acta. 57:403-414.
    • (1974) Helvetica Chimica Acta , vol.57 , pp. 403-414
    • Marbach, P.1    Rudinger, J.2
  • 18
    • 1842555216 scopus 로고    scopus 로고
    • Ion channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by barrel-stave model
    • Matsubara, A., K. Asami, A. Akagi, and N. Nishino. 1996. Ion channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by barrel-stave model. J. Chem. Soc. Chem. Commun. 2069-2070.
    • (1996) J. Chem. Soc. Chem. Commun. , pp. 2069-2070
    • Matsubara, A.1    Asami, K.2    Akagi, A.3    Nishino, N.4
  • 19
    • 0014428197 scopus 로고
    • Action potentials induced in bimolecular lipid membranes
    • Mueller, P., and D. O. Rudin. 1968. Action potentials induced in bimolecular lipid membranes. Nature. 217:713-719.
    • (1968) Nature , vol.217 , pp. 713-719
    • Mueller, P.1    Rudin, D.O.2
  • 20
    • 0037615140 scopus 로고    scopus 로고
    • Ion channel properties of disulfide-linked dimer derivatives of peptaibol, trichosporin-B-Via
    • Nagaoka, Y., A. Iida, S. Hatanaka, K. Tomioka, K. Asami, and T. Fujita. 1996a. Ion channel properties of disulfide-linked dimer derivatives of peptaibol, trichosporin-B-Via. Pept. Chem. 34:189-192.
    • (1996) Pept. Chem. , vol.34 , pp. 189-192
    • Nagaoka, Y.1    Iida, A.2    Hatanaka, S.3    Tomioka, K.4    Asami, K.5    Fujita, T.6
  • 21
    • 0030583218 scopus 로고    scopus 로고
    • Role of proline residue in the channel-forming and catecholamine-releasing activities of the peptaibol, trichosporin-B-Via
    • Nagaoka, Y., A. Iida, T. Kambara, K. Asami, E. Tachikawa, and T. Fujita. 1996b. Role of proline residue in the channel-forming and catecholamine-releasing activities of the peptaibol, trichosporin-B-Via. Biochim. Biophys. Acta. 1283:31-36.
    • (1996) Biochim. Biophys. Acta , vol.1283 , pp. 31-36
    • Nagaoka, Y.1    Iida, A.2    Kambara, T.3    Asami, K.4    Tachikawa, E.5    Fujita, T.6
  • 22
    • 0025935264 scopus 로고
    • The biophysics of peptide models of ion channels
    • Sansom, M. S. P. 1991. The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 55:139-235.
    • (1991) Prog. Biophys. Mol. Biol. , vol.55 , pp. 139-235
    • Sansom, M.S.P.1
  • 23
    • 0020172089 scopus 로고
    • Structural and dipolar properties of the voltage-dependent pore former alamethicin in octanol/dioxane
    • Schwarz, G., and P. Savko. 1982. Structural and dipolar properties of the voltage-dependent pore former alamethicin in octanol/dioxane. Biophys. J. 39:211-219.
    • (1982) Biophys. J. , vol.39 , pp. 211-219
    • Schwarz, G.1    Savko, P.2
  • 24
    • 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
  • 27
    • 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
  • 28
    • 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.