{"title":"研究双孔通道孔隙突变体。","authors":"Christopher J Penny, Sandip Patel","doi":"10.1166/msr.2015.1044","DOIUrl":null,"url":null,"abstract":"<p><p>Two-pore channels are members of the voltage-gated ion channel superfamily. They localise to the endolysosomal system and are likely targets for the Ca<sup>2+</sup> mobilising messenger NAADP. In this brief review, we relate mutagenesis of the TPC pore to a recently published homology model and discuss how pore mutants are informing us of TPC function. Molecular physiology of these ubiquitous proteins is thus emerging.</p>","PeriodicalId":74176,"journal":{"name":"Messenger (Los Angeles, Calif. : Print)","volume":" ","pages":"46-52"},"PeriodicalIF":0.0000,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1166/msr.2015.1044","citationCount":"4","resultStr":"{\"title\":\"Poring over two-pore channel pore mutants.\",\"authors\":\"Christopher J Penny, Sandip Patel\",\"doi\":\"10.1166/msr.2015.1044\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Two-pore channels are members of the voltage-gated ion channel superfamily. They localise to the endolysosomal system and are likely targets for the Ca<sup>2+</sup> mobilising messenger NAADP. In this brief review, we relate mutagenesis of the TPC pore to a recently published homology model and discuss how pore mutants are informing us of TPC function. Molecular physiology of these ubiquitous proteins is thus emerging.</p>\",\"PeriodicalId\":74176,\"journal\":{\"name\":\"Messenger (Los Angeles, Calif. : Print)\",\"volume\":\" \",\"pages\":\"46-52\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2015-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1166/msr.2015.1044\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Messenger (Los Angeles, Calif. : Print)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1166/msr.2015.1044\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Messenger (Los Angeles, Calif. : Print)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1166/msr.2015.1044","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Two-pore channels are members of the voltage-gated ion channel superfamily. They localise to the endolysosomal system and are likely targets for the Ca2+ mobilising messenger NAADP. In this brief review, we relate mutagenesis of the TPC pore to a recently published homology model and discuss how pore mutants are informing us of TPC function. Molecular physiology of these ubiquitous proteins is thus emerging.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
