首页> 外文期刊>American Journal of Physiology >CFTR channel pharmacology: Insight from a flock of clones. focus on 'divergent CFTR orthologs respond differently to the channel inhibitors CFTR inh-172, glibenclamide, and GlyH-101'
【24h】

CFTR channel pharmacology: Insight from a flock of clones. focus on 'divergent CFTR orthologs respond differently to the channel inhibitors CFTR inh-172, glibenclamide, and GlyH-101'

机译:CFTR通道药理学:来自众多克隆的见解。专注于“不同的CFTR直系同源物对通道抑制剂CFTR inh-172,格列本脲和GlyH-101的反应不同”

获取原文
获取原文并翻译 | 示例
           

摘要

how do you identify drug-binding sites on an ion channel when you don't have a crystal structure? In the case of the cystic fibrosis transmembrane conductance regulator (CFTR), which plays a pivotal role in transepithelial ion transport, several approaches have been tried, including 1) targeting functionally important residues (4), 2) alanine-scanning mutagenesis (1), and 3) docking drugs with molecular models of isolated domains (6). In this issue of the American Journal of Physiology-Cell Physiology, an alternative approach is suggested by work from John Forrest Jr.'s group (9).
机译:当您没有晶体结构时,如何识别离子通道上的药物结合位点?对于囊性纤维化跨膜电导调节剂(CFTR),它在跨上皮离子转运中起关键作用,已经尝试了多种方法,包括1)靶向功能重要的残基(4),2)丙氨酸扫描诱变(1) ,以及3)将药物与孤立域的分子模型对接(6)。在本期《美国生理学-细胞生理学杂志》上,约翰·福雷斯特(John Forrest Jr.)小组的工作提出了一种替代方法(9)。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号