4.7 Editorial Material

Closing In on the Hsp90 Chaperone-Client Relationship

期刊

STRUCTURE
卷 19, 期 4, 页码 445-446

出版社

CELL PRESS
DOI: 10.1016/j.str.2011.03.007

关键词

-

向作者/读者索取更多资源

The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据