期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 47, 期 12, 页码 1038-1047出版社
CELL PRESS
DOI: 10.1016/j.tibs.2022.06.009
关键词
-
资金
- NIH [R01GM111639, R01GM115844]
- Michael J. Fox Foundation
- National Natural Science Foundation of China (NSFC) [81971196]
This review discusses new insights gained from recent cryo-EM structures of LRRK2, aiming to understand its mechanisms of action and explore potential new therapeutic avenues.
Mutation in leucine-rich repeat (LRR) kinase 2 (LRRK2) is a common cause of Parkinson's disease (PD). Aberrant LRRK2 kinase activity is associated with disease pathogenesis and thus it is an attractive drug target for combating PD. Intense efforts in the past nearly two decades have focused on the development of small-molecule inhibitors of the kinase domain of LRRK2 and have identified potent kinase inhibitors. However, most LRRK2 kinase inhibitors have shown adverse effects; therefore, alternative-mechanism-based strategies are desperately needed. In this review, we discuss the new insights gleaned from recent cryoelectron microscope (cryo-EM) structures of LRRK2 towards understanding the mechanisms of actions of LRRK2 and explore the potential new therapeutic avenues.
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。
推荐
暂无数据