Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers
- 1 November 1989
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 56 (5), 1017-1021
- https://doi.org/10.1016/s0006-3495(89)82746-8
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Antimicrobial properties of peptides from Xenopus granular gland secretionsFEBS Letters, 1988
- Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.Proceedings of the National Academy of Sciences, 1987
- Comparison of the conformation and orientation of alamethicin and melittin in lipid membranesBiochemistry, 1987
- Single chloride-permeable channels of large conductance in cultured cardiac cells of new-born ratsEuropean Biophysics Journal, 1987
- Interactions between membranes and cytolytic peptidesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1986
- A large anion-selective channel has seven conductance levelsNature, 1986
- Alamethicin. A rich model for channel behaviorBiophysical Journal, 1984
- Open-state substructure of single chloride channels from Torpedo electroplaxPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1982
- A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolutionNature, 1982
- Statistical analysis of alamethicin channels in black lipid membranesThe Journal of Membrane Biology, 1974