WU Jingxiang
Work Experience
2022-present, Principal Investigator, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College.
2018-2021, Postdoctoral fellow , Institute of Molecular Medicine, Peking University
2016-2018, Postdoctoral fellow , Institute of Molecular Medicine, Peking University
Education
2016 Ph. D. Biology, School of Life Sciences, Tsinghua University, Beijing, China
2009 B. Sc. Biology, School of Life Sciences, Hunan Normal University, Changsha, China
Functional proteins are essential to our life and health. For the personalized medicine, it is essential to understand the detailed mechanism of target protein. Wu Jing-Xiang has been committed to study the working mechanism of biologically important membrane proteins and enzymes, especially proteins related to diabetes, nephropathy, neurodegenerative diseases and immunodeficiency. She aims to elucidate the fundamental relationship between protein structure and function, the pathogenic mechanism of related genetic mutations and the pharmacological mechanism of small molecules or drugs for new drug discovery. She has published more than 20 papers on Cell, Nature Communications, Nature, etc . Her studies have gained considerable attention in the research area and some of her researches have been cited more than 100 times by other researchers.
1. Wu, Jing-Xiang, Ding, Dian, Chen, Lei. The Emerging Structural Pharmacology of ATP-Sensitive Potassium Channels. Mol Pharmacol, 2022, 102(5): 234-239.
2. Wu, Jing-Xiang, Liu, Rui, Song, Kangcheng, Chen, Lei. Structures of human dual oxidase 1 complex in low-calcium and high-calcium states. Nat Commun, 2021, 12(1): 155.
3. Wu, Jing-Xiang, Ding, Dian, Wang, Mengmeng, Chen, Lei. Structural Insights into the Inhibitory Mechanism of Insulin Secretagogues on the Pancreatic ATP-Sensitive Potassium Channel. Biochemistry (Mosc), 2020, 59(1): 18-25.
4. Wu, Jing-Xiang, Chen, Lei. Recent Progress on The Studies of OSCA/TMEM63 Family Ion Channels. Progress in Biochemistry and Biophysics, 2020, 47(2): 123-130.
5. Ding, Dian(#), Wang, Mengmeng(#), Wu, Jing-Xiang(#), Kang, Yunlu, Chen, Lei. The Structural Basis for the Binding of Repaglinide to the Pancreatic KATP Channel. Cell Rep, 2019, 27(6): 1848-1857 e1844.
6. Wu, Jing-Xiang, Ding, Dian, Wang, Mengmeng, Kang, Yunlu, Zeng, Xin, Chen, Lei. Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels. Protein Cell, 2018, 9(6): 553-567.
7. Li, Ningning(#), Wu, Jing-Xiang(#), Ding, Dian, Cheng, Jiaxuan, Gao, Ning, Chen, Lei. Structure of a Pancreatic ATP-Sensitive Potassium Channel. Cell, 2017, 168(1-2): 101-110 e110.
8. Ma, Hui(#), Wu, Jing-Xiang(#), Wang, Jue, Wang, Zhi-Xin, Wu, Jia-Wei. Structure and inhibition analysis of the mouse SAD-B C-terminal fragment. Bioscience Biotechnology and Biochemistry, 2016, 80(10): 1939-1946.
9. Wu, Jing-Xiang, Cheng, Yun-Sheng, Wang, Jue, Chen, Lei, Ding, Mei, Wu, J. W. Structural insight into the mechanism of synergistic autoinhibition of SAD kinases. Nature Communications, 2015, 6.
10. Tang, Qinglin(#), Guo, Wenjun(#), Zheng, Li, Wu, Jing-Xiang, Liu, Meng, Zhou, Xindi, Zhang, Xiaolin, Chen, Lei. Structure of the receptor-activated human TRPC6 and TRPC3 ion channels. Cell Res, 2018, 28(7): 746-755.
11. Zhang, Mingfeng, Wang, Dali, Kang, Yunlu, Wu, Jing-Xiang, Yao, Fuqiang, Pan, Chengfang, Yan, Zhiqiang, Song, Chen, Chen, Lei. Structure of the mechanosensitive OSCA channels. Nat Struct Mol Biol, 2018, 25(9): 850-858.
12. Kang, Yunlu(#), Liu, Rui(#), Wu, Jing-Xiang, Chen, Lei. Structural insights into the mechanism of human soluble guanylate cyclase. Nature, 2019, 574(7777): 206-210.
13. Guan, Chengcheng, Niu, Yange, Chen, Si-Cong, Kang, Yunlu, Wu, Jing-Xiang, Nishi, Koji, Chang, Catherine C. Y., Chang, Ta-Yuan, Luo, Tuoping, Chen, Lei. Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor. Nature Communications, 2020, 11(1).
14. Kang, Yunlu, Wu, Jing-Xiang, Chen, Lei. Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex. Nat Commun, 2020, 11(1): 6199.
15. Song, Kangcheng(#), Wei, Miao(#), Guo, Wenjun, Quan, Li, Kang, Yunlu, Wu, Jing-Xiang, Chen, Lei. Structural basis for human TRPC5 channel inhibition by two distinct inhibitors. Elife, 2021, 10.
16. Ding, Dian, Wu, Jing-Xiang, Duan, Xinli, Ma, Songling, Lai, Lipeng, Chen, Lei. Structural identification of vasodilator binding sites on the SUR2 subunit. Nat Commun, 2022, 13(1): 2675.
17. Guo, Wenjun, Tang, Qinglin, Wei, Miao, Kang, Yunlu, Wu, Jing-Xiang, Chen, Lei. Structural mechanism of human TRPC3 and TRPC6 channel regulation by their intracellular calcium-binding sites. Neuron, 2022, 110(6): 1023-1035.
18. Wang, Mengmeng, Wu, Jing-Xiang, Chen, Lei. Structural Insights Into the High Selectivity of the Anti-Diabetic Drug Mitiglinide. Frontiers in Pharmacology, 2022, 13.
19. Wang, Mengmeng, Wu, Jing-Xiang, Ding, Dian, Chen, Lei. Structural insights into the mechanism of pancreatic K-ATP channel regulation by nucleotides. Nature Communications, 2022, 13(1).
20. Liu, Rui(#), Song, Kangcheng(#), Wu, Jing-Xiang, Geng, Xiao-Peng, Zheng, Liming, Gao, Xiaoyin, Peng, Hailin, Chen, Lei, Structure of human phagocyte NADPH oxidase in the resting state. Elife, 2022, 11.
