1.    Ji, Tuo, Ge, Piao, Zhang, Shan, Wan, Chanjuan, Liu, Hailong, Qu, Xiaozhan, Zhu, Feng, Gong, Qingguo, Xu, Weiya, Wang, Chao#, Wang, Yucai#, and Huang, Chengdong#. Remote On-Off Switching of Protein Activity by Intrinsically Disordered Region. Nat. Struct. Mol. Biol. (in press)

2.    Qu, Xiaozhan; Zhao, Shuo; Wan, Chanjuan; Zhu, Lei; Ji, Tuo; Rossi, Paolo; Wang, Junfeng; Kalodimos, Charalampos G.; Wang, Chao; Xu, Weiya#; Huang, Chengdong#. Structural basis for the dynamic chaperoning of disordered clients by Hsp90. Nat. Struct. Mol. Biol. (2024) 31(10):1482-1491.

3.    Qu, Xiaozhan; Wang, Simin; Zhao, Shuo; Wan, Chanjuan; Xu, Weiya#; Huang, Chengdong#. The Dynamic Triage Interplay of Hsp90 with its Chaperone Cycle and Client Binding. Nat.Commun. (2024) 15(1):10661.

4.    Kong, Chao; Qu, Xiaozhan; Liu, Mingming; Xu, Weiya; Chen, Da; Zhang, Yanshen; Zhang, Shan; Zhu, Feng; Liu, Zhenbang; Li, Jianchao; Huang, Chengdong#; Wang, Chao#. Dynamic interactions between E-cadherin and Ankyrin-G mediate epithelial cell polarity maintenance. Nat. Commun. 2023;14(1):6860.

5.    Li, Hang; Ji, Tuo, Sun, Qi; Chen, Yao, Xu, Weiya#; Huang, Chengdong#. Structural insights into selective inhibition of leishmanial GDP-mannose pyrophosphorylase. Cell Discov. (2022) 8(1):83.

6.    Chen, Yao; Xu, Weiya; Yu, Shuwei; Ni, Kang; She, Guangbiao; Ye, Xiaodong; Xing, Qiong#; Zhao, Jian#; Huang, Chengdong#. Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme. Elife (2021) 10:e72535.

7.    Huang, Chengdong; Rossi, Paolo; Saio, Tomohide; Kalodimos, Charalampos, G. Structural basis for the antifolding activity of a molecular chaperone. Nature. (2016) 537, 202-206.