当前位置: X-MOL 学术Angew. Chem. Int. Ed. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Frontispiece: Mechanism-Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure–Activity Relationship, Biostructural, and Kinetic Insight
Angewandte Chemie International Edition ( IF 16.6 ) Pub Date : 2017-11-15 06:53:57 , DOI: 10.1002/anie.201784761
Nima Rajabi 1 , Marina Auth 1 , Kathrin R. Troelsen 1 , Martin Pannek 2 , Dhaval P. Bhatt 3 , Martin Fontenas 1 , Matthew D. Hirschey 3 , Clemens Steegborn 2 , Andreas S. Madsen 1 , Christian A. Olsen 1
Affiliation  

Medicinal Chemistry C. A. Olsen and co-workers describe the identification of inhibitors of sirtuin 5 hydrolase with high potencies through an extensive structure–activity relationship study in their Communication on page 14836 ff.

中文翻译:

代表作:人类Sirtuin 5脱酰基酶的基于机制的抑制剂:结构与活性的关系,生物结构和动力学见解

药物化学C. A. Olsen及其同事在其第14836页及其后的通讯中,通过广泛的结构-活性关系研究,描述了高活性的瑟土因5水解酶抑制剂的鉴定
更新日期:2017-11-15
down
wechat
bug