메뉴 건너뛰기




Volumn 72, Issue 5, 1997, Pages 2151-2159

Influence of proline position upon the ion channel activity of alamethicin

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; ION CHANNEL;

EID: 0030896697     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78858-1     Document Type: Article
Times cited : (37)

References (34)
  • 1
    • 0025832273 scopus 로고
    • Dynamics and aggregation of the peptide ion channel alamethicin
    • Archer, S. J., J. E. Ellena, and D. S. Cafiso. 1991. Dynamics and aggregation of the peptide ion channel alamethicin. Biophys. J. 60:389-398.
    • (1991) Biophys. J. , vol.60 , pp. 389-398
    • Archer, S.J.1    Ellena, J.E.2    Cafiso, D.S.3
  • 2
    • 0030024628 scopus 로고    scopus 로고
    • Membran structure of voltage gated ion channel forming peptides by side-directed spin labeling
    • Barranger-Mathys, M., and D. S. Cafiso. 1996. Membran structure of voltage gated ion channel forming peptides by side-directed spin labeling. Biochemistry. 35:498-505.
    • (1996) Biochemistry , vol.35 , pp. 498-505
    • Barranger-Mathys, M.1    Cafiso, D.S.2
  • 3
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • Baumann, G., and P. Mueller. 1974. A molecular model of membrane excitability. J. Supramol. Struct. 2:538-557.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 4
    • 0016183539 scopus 로고
    • Statistical analysis of alamethicin channels in black lipid membranes
    • Boheim, G. 1974. Statistical analysis of alamethicin channels in black lipid membranes. J. Membr. Biol 19:277-303.
    • (1974) J. Membr. Biol , vol.19 , pp. 277-303
    • Boheim, G.1
  • 5
    • 0028931843 scopus 로고
    • Conformational study of a synthetic analogue of alamethicin
    • Brachais, L., D. Davoust, and G. Molle. 1995a. Conformational study of a synthetic analogue of alamethicin. Int. J. Pept. Protein Res. 45:164-172.
    • (1995) Int. J. Pept. Protein Res. , vol.45 , pp. 164-172
    • Brachais, L.1    Davoust, D.2    Molle, G.3
  • 6
    • 0029157274 scopus 로고
    • Influence of proline-14 substitution on the secondary structure in a synthetic analogue of alamethicin
    • Brachais, L., H. Duclohier, C. Mayer, D. Davoust, and G. Molle. 1995b. Influence of proline-14 substitution on the secondary structure in a synthetic analogue of alamethicin. Biopolymers. 36:547-558.
    • (1995) Biopolymers , vol.36 , pp. 547-558
    • Brachais, L.1    Duclohier, H.2    Mayer, C.3    Davoust, D.4    Molle, G.5
  • 7
    • 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
  • 9
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by CD and optical rotary dispersion
    • Chen, Y. H., J. T. Yang, and H. M. Martinez. 1972. Determination of the secondary structures of proteins by CD and optical rotary dispersion. Biochemists. 11:4120-4131.
    • (1972) Biochemists , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 10
    • 0026673421 scopus 로고
    • Proline are not essential residues in the "barrel-stave" model for ion channels induced by alamethicin analogues
    • Duclohier, H., G. Molle, J.-Y. Dugast, and G. Spach. 1992. Proline are not essential residues in the "barrel-stave" model for ion channels induced by alamethicin analogues. Biophys. J. 63:868-873.
    • (1992) Biophys. J. , vol.63 , pp. 868-873
    • Duclohier, H.1    Molle, G.2    Dugast, J.-Y.3    Spach, G.4
  • 12
    • 0020360086 scopus 로고
    • A voltage gated ion channel model inferred from the cristal structure of alamethicin at 1.5 Å resolution
    • Fox, F. O., and F. M. Richards. 1982. A voltage gated ion channel model inferred from the cristal structure of alamethicin at 1.5 Å resolution. Nature. 300:325-330.
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox, F.O.1    Richards, F.M.2
  • 14
    • 0025614191 scopus 로고
    • Restrained and unrestrained molecular dynamics simultation in the NVT ensemble of alamethicin
    • Fraternali, F. 1990. Restrained and unrestrained molecular dynamics simultation in the NVT ensemble of alamethicin. Biopolymers. 30: 1083-1099.
    • (1990) Biopolymers , vol.30 , pp. 1083-1099
    • Fraternali, F.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
    • 0016848186 scopus 로고
    • Potential-dependent conductance in lipid membranes containing alamethicin
    • Gordon, L. G. M., and D. A. Haydon. 1975. Potential-dependent conductance in lipid membranes containing alamethicin. Phil. Trans. R. Soc. London Ser. B. 270:433-447.
    • (1975) Phil. Trans. R. Soc. London Ser. B , vol.270 , pp. 433-447
    • Gordon, L.G.M.1    Haydon, D.A.2
  • 18
    • 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
  • 20
    • 0026772321 scopus 로고
    • Determination of the molecular dynamics of alamethicin using 13C NMR: Implications for the mechanism of gating of a voltage-dependent channel
    • Kelsh, J. P., J. F. Ellena, and D. S. Cafiso. 1992. Determination of the molecular dynamics of alamethicin using 13C NMR: implications for the mechanism of gating of a voltage-dependent channel. Biochemistry. 31:5136-5144.
    • (1992) Biochemistry , vol.31 , pp. 5136-5144
    • Kelsh, J.P.1    Ellena, J.F.2    Cafiso, D.S.3
  • 21
    • 0014203489 scopus 로고
    • A polypeptide antibacterial agent isolated from Trichoderma viride
    • Meyer, P., and F. Reusser. 1967. A polypeptide antibacterial agent isolated from Trichoderma viride. Experientia. 23:85-86.
    • (1967) Experientia , vol.23 , pp. 85-86
    • Meyer, P.1    Reusser, F.2
  • 22
    • 0029913429 scopus 로고    scopus 로고
    • Ion channel stabilization of synthetic alamethicin analogs by rings of imer-helix H-bounds
    • Molle, G., J.-Y. Dugast, G. Spach, and H. Duclohier. 1996. Ion channel stabilization of synthetic alamethicin analogs by rings of imer-helix H-bounds. 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
  • 23
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from monolayers and study of their properties
    • Montal, M., and P. Mueller. 1972. Formation of bimolecular membranes from monolayers and study of their properties. Proc. Natl. Acad. Sci. USA. 69:3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 24
    • 0028033914 scopus 로고
    • Molecular flexibility demonstrated by paramagnetic enhancement of nuclear relaxation. Application to alamethicin
    • North, Ch. L., J. C. Frankline, R. G. Bryant, and D. S. Cafiso. 1994. Molecular flexibility demonstrated by paramagnetic enhancement of nuclear relaxation. Application to alamethicin. Biophys. J. 67: 1861-1866.
    • (1994) Biophys. J. , vol.67 , pp. 1861-1866
    • North, Ch.L.1    Frankline, J.C.2    Bryant, R.G.3    Cafiso, D.S.4
  • 25
    • 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
  • 26
    • 0027817476 scopus 로고
    • Structure and function of channel forming peptaibols
    • Sansom, M. S. P. 1993. 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
  • 28
    • 0023248806 scopus 로고
    • Comparison of the conformation and orientation of alamethicin and mellitin in lipid membranes
    • Vogel, H. 1987. Comparison of the conformation and orientation of alamethicin and mellitin in lipid membranes. Biochemistry. 26:4562-4572.
    • (1987) Biochemistry , vol.26 , pp. 4562-4572
    • Vogel, H.1
  • 29
    • 0027398959 scopus 로고
    • Structural fluctuations between two conformational states of a transmembrane helical peptide related to its channel-forming properties in planar lipid membranes
    • Vogel, H., L. Nilsson, R. Riegler, S. Meder, G. Boheim, W. Beck, H.-H. Kurth, and G. Jung. 1993. Structural fluctuations between two conformational states of a transmembrane helical peptide related to its channel-forming properties in planar lipid membranes. Eur. J. Biochem. 212: 305-313.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 305-313
    • Vogel, H.1    Nilsson, L.2    Riegler, R.3    Meder, S.4    Boheim, G.5    Beck, W.6    Kurth, H.-H.7    Jung, G.8
  • 31
    • 0025801502 scopus 로고
    • Conserved positioning of proline residue in membrane-spanning helices of ion channel proteins
    • Woolfson, D. N., R. J. Mortishire-Smith, and D. H. Williams. 1991. Conserved positioning of proline residue in membrane-spanning helices of ion channel proteins. Biochem. Biophys. Res. Commun. 175:733-737.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 733-737
    • Woolfson, D.N.1    Mortishire-Smith, R.J.2    Williams, D.H.3
  • 32
    • 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
  • 33
    • 0028823379 scopus 로고
    • The conformation of an alamethicin in methanol by multinuclear NMR specroscopy and distance geometry/stimulated annealing
    • Yee, A. A., R. Babiuk, and J. D. J. O'Neil. 1995. The conformation of an alamethicin in methanol by multinuclear NMR specroscopy and distance geometry/stimulated annealing. Biopolymers. 36:781-792.
    • (1995) Biopolymers , vol.36 , pp. 781-792
    • Yee, A.A.1    Babiuk, R.2    O'Neil, J.D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.