{"title":"蝎子的毒素和防御素。","authors":"M Goyffon, C Landon","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The scorpion venoms possess many neurotoxic peptides which constitute a group of molecular families with a common architecture and a high degree of polymorphism. This architecture is found also in circulating antimicrobial peptides belonging to the defensins family, which are especially structurally related to the blocking potassium channels neurotoxins. The diversification in functions with a unique architectural scheme is discussed taking in account the biophysiological characteristics of the scorpion order.</p>","PeriodicalId":10658,"journal":{"name":"Comptes rendus des seances de la Societe de biologie et de ses filiales","volume":"192 3","pages":"445-62"},"PeriodicalIF":0.0000,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Scorpion toxins and defensins].\",\"authors\":\"M Goyffon, C Landon\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The scorpion venoms possess many neurotoxic peptides which constitute a group of molecular families with a common architecture and a high degree of polymorphism. This architecture is found also in circulating antimicrobial peptides belonging to the defensins family, which are especially structurally related to the blocking potassium channels neurotoxins. The diversification in functions with a unique architectural scheme is discussed taking in account the biophysiological characteristics of the scorpion order.</p>\",\"PeriodicalId\":10658,\"journal\":{\"name\":\"Comptes rendus des seances de la Societe de biologie et de ses filiales\",\"volume\":\"192 3\",\"pages\":\"445-62\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comptes rendus des seances de la Societe de biologie et de ses filiales\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comptes rendus des seances de la Societe de biologie et de ses filiales","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The scorpion venoms possess many neurotoxic peptides which constitute a group of molecular families with a common architecture and a high degree of polymorphism. This architecture is found also in circulating antimicrobial peptides belonging to the defensins family, which are especially structurally related to the blocking potassium channels neurotoxins. The diversification in functions with a unique architectural scheme is discussed taking in account the biophysiological characteristics of the scorpion order.