The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation-论文-万方医学网

The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation

导出原文传递

翻译打印收藏纠错

作者： Salaun, Christine ^[1] ; Greaves, Jennifer ^[2] ; Tomkinson, Nicholas C. O. ^[3] ; Chamberlain, Luke H.

作者单位： Univ Strathclyde, Strathclyde Inst Pharm & Biomed Sci, 161 Cathedral St, Glasgow G4 0RE, Lanark ^[1] Coventry Univ, Fac Hlth & Life Sci, Ctr Sport Exercise & Life Sci, Coventry CV1 5FB, W Midlands ^[2] Univ Strathclyde, Dept Pure & Appl Chem, WestCHEM, Glasgow G1 1XL, Lanark, Scotland ^[3]

关键词 protein palmitoylation post-translational modification (PTM)protein acylation protein chemical modification protein domain ankyrin repeat domain mPEG-click S-acylation zDHHC enzyme zDHHC17

发布时间 2022-09-11

翻译满意度评价：

准确一般字义偏差语意偏离译文作用小提交

浏览0

相似文献

中文期刊
外文期刊
学位论文
会议论文

检索历史清除

The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation

相似文献

相关期刊

参考文献：
指定格式：	NoteExpress EndNote RefWorks NoteFirst

检索历史 清除

The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation

相似文献

相关期刊

检索历史清除