Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin.
Bechinger
B
B
Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany.
D000408:Alamethicin / Q000737:chemistry* / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D002463:Cell Membrane Permeability / Q000187:drug effects; D004734:Energy Metabolism; D019476:Insect Proteins / Q000737:chemistry* / Q000494:pharmacology / Q000502:physiology; D007473:Ion Channels / Q000737:chemistry*; D008051:Lipid Bilayers; D054806:Magainins; D008555:Melitten / Q000737:chemistry* / Q000494:pharmacology / Q000502:physiology; D008564:Membrane Potentials / Q000187:drug effects; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology / Q000502:physiology; D012756:Sheep; D013329:Structure-Activity Relationship; D029867:Xenopus Proteins
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D054806:Magainins; D010455:Peptides; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus; D008555:Melitten; D000408:Alamethicin; C031161:cecropin A