Biography

Education

1995/09-1998/06: Wuhan University, PhD;

1985/09-1988/06: Wuhan University, Master’s Degree;

1981/09-1985/06: Wuhan University, Bachelor’s Degree

Professional Experience

2001/12-: Full Professor, College of Life Sciences, Wuhan University;

2022/07: Principal Investigator, TaiKang Center for Life and Medical Sciences, Wuhan University;

2013/11-2013/12: Invited Professor, University of Michigan, USA;

2008/05-2008/08 and 2006/01-2007/02: Invited Professor, National Institutes of Health, USA;

2001/12-2002/03: Invited Professor, CNRS, Université Louis Pasteur

2001/01-2001/11: Associate Professor, College of Life Sciences, Wuhan University;

1998/07-2000/12: Postdoctoral Fellow in Biochemistry, Institute of Biophysics, the Chinese Academy of Sciences;

1996/01-1998/06: Associate Professor, School of Chemical Engineering and Pharmacy, Wuhan Institute of Chemical Technology;

1988/07-1995/12: Instructor, School of Chemical Engineering and Pharmacy, Wuhan Institute of Chemical Technology

Research

Prion diseases primarily caused by the conformational conversion of prion protein (PrP) from its cellular form (PrPC) into a pathological aggregated form (PrPSc) in humans, cattle, sheep and cervid species. A major pathological hallmark of Amyotrophic lateral sclerosis (ALS) is the aggregates formed by copper, zinc superoxide dismutase (SOD1) in motor neuron cells. Yi Liang and colleagues produced amyloid fibrils in vitro from recombinant, full-length human PrPC (residues 23–231) and determined their structure using cryo-electron microscopy (cryo-EM), building a model for the fibril core comprising residues 170-229. The Liang laboratory also produced cytotoxic amyloid fibrils from full-length apo human SOD1 and determined the atomic structure using cryo-EM. The SOD1 fibril core exhibits a serpentine fold comprising N-terminal segment (residues 3 to 55) and C-terminal segment (residues 86 to 153). By comparison with the structure of PrPC, Liang and co-workers propose that two a-helices in the C-terminal domain of PrPC convert into b-strands in the PrP fibril. By comparison with the structure of apo SOD1 dimer, Liang and colleagues also propose that eight b-strands (to form a b-barrel) and one a-helix in the subunit of apo SOD1 convert into thirteen b-strands in the SOD1 fibril. These data provide structural insights into the conversion of PrP and SOD1 between physiological and pathological states, also provide structural evidences of the diverse prion strains or SOD1 strains and highlight the importance of familial mutations in inducing different strains.

Representative  Publications

1. Li-Qiang Wang^#, Kun Zhao^#, Han-Ye Yuan, Qiang Wang, Zeyuan Guan, Jing Tao, Xiang-Ning Li, Yunpeng Sun, Chuan-Wei Yi, Jie Chen, Dan Li, Delin Zhang, Ping Yin, Cong Liu^*, Yi Liang^*. Cryo-EM structure of an amyloid fibril formed by full-length human prion protein. Nature Structural & Molecular Biology 2020 Jun, 27(6), 598-602.

2. Li-Qiang Wang^#, Kun Zhao^#, Han-Ye Yuan^#, Xiang-Ning Li, Hai-Bin Dang, Yeyang Ma, Qiang Wang, Chen Wang, Yunpeng Sun, Jie Chen, Dan Li, Delin Zhang, Ping Yin, Cong Liu^*, Yi Liang^*. Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM. Science Advances 2021 Sep 10, 7(37), eabg9676.

3. Li-Qiang Wang^#, Yeyang Ma^#, Han-Ye Yuan^#, Kun Zhao, Mu-Ya Zhang, Qiang Wang, Xi Huang, Wen-Chang Xu, Bin Dai, Jie Chen, Dan Li, Delin Zhang, Zhengzhi Wang, Liangyu Zou, Ping Yin, Cong Liu^*, Yi Liang^*. Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion. Nature Communications 2022 Jun 17, 13(1), 3491.

4. Wen-Chang Xu^#, Jin-Zhao Liang, Cheng Li, Zhi-Xin He, Han-Ye Yuan, Ben-Yan Huang, Xiao-Ling Liu, Bo Tang, Dai-Wen Pang, Hai-Ning Du, Yi Yang, Jie Chen, Lei Wang, Min Zhang^*, Yi Liang^*. Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111. Cell Death Dis. 2018 Jan 22, 9(2), 67.

5. Kan Wang^#, Jia-Qi Liu#, Tao Zhong, Xiao-Ling Liu, Yan Zeng, Xinhua Qiao, Ting Xie, Yuzhe Chen, Ying-Ying Gao, Bo Tang, Jia Li, Jun Zhou, Dai-Wen Pang, Jie Chen, Chang Chen, Yi Liang^*. Phase separation and cytotoxicity of Tau are modulated by protein disulfide isomerase and S-nitrosylation of this molecular chaperone. J. Mol. Biol. 2020 Mar 27, 432(7), 2141-2163.

6. Jun-Jie Huang^#, Xiang-Ning Li^#, Wan-Li Liu, Han-Ye Yuan, Yuan Gao, Kan Wang, Bo Tang, Dai-Wen Pang, Jie Chen, Yi Liang^*. Neutralizing mutations significantly inhibit amyloid formation by human prion protein and decrease its cytotoxicity. J. Mol. Biol. 2020 Feb 14, 432(4), 828-844.

7. Xinxin Zuo^#, Jie Zhou^#, Yinming Li^#, Kai Wu, Zonggui Chen, Zhiwei Luo, Xiaorong Zhang, Yi Liang, Miguel A. Esteban, Yu Zhou^*, Xiang-Dong Fu^*. TDP-43 aggregation induced by oxidative stress causes global mitochondrial imbalance in ALS. Nature Structural & Molecular Biology 2021 Feb, 28(2), 132-142.

8. Bin Dai^#, Tao Zhong, Zhi-Xian Chen, Wang Chen, Na Zhang, Xiao-Ling Liu, Li-Qiang Wang, Jie Chen, Yi Liang^*. Myricetin slows liquid-liquid phase separation of Tau and activates ATG5-dependent autophagy to suppress Tau toxicity. J. Biol. Chem. 2021 Oct, 297(4), 101222.

9. Xiang-Ning Li^#, Yuan Gao^#, Yang Li, Jin-Xu Yin, Chuan-Wei Yi, Han-Ye Yuan, Jun-Jie Huang, Li-Qiang Wang, Jie Chen, Yi Liang^*. Arg177 and Asp159 from dog prion protein slow liquid–liquid phase separation and inhibit amyloid formation of human prion protein. J. Biol. Chem. 2023 Nov, 299(11), 105329.

10. Ying-Ying Gao^#, Tao Zhong^#, Li-Qiang Wang, Na Zhang, Yan Zeng, Ji-Ying Hu, Hai-Bin Dang, Jie Chen, Yi Liang^*. Zinc enhances liquid-liquid phase separation of Tau protein and aggravates mitochondrial damages in cells. Int. J. Biol. Macromol. 2022 Jun 1 209(Pt A), 703-715.

11. Tianxin Xie^#, Yuying Li, Chuan Tian, Chang Yuan, Bin Dai, Shubo Wang, Kaixiang Zhou, Jiaqi Liu, Hongwei Tan, Yi Liang^*, Jiapei Dai, Baian Chen^*, Mengchao Cui^*. Fused cycloheptatriene–BODIPY is a high-performance near-infrared probe to image Tau tangles. J. Med. Chem. 2022 Nov 10, 65(21), 14527-14538.

12. Kaixiang Zhou^#, Chang Yuan, Bin Dai, Kan Wang, Yimin Chen, Denglei Ma, Jiapei Dai, Yi Liang^*, Hongwei Tan^*, Mengchao Cui^*. Environment-sensitive near-infrared probe for fluorescent discrimination of Ab and Tau fibrils in AD brain. J. Med. Chem. 2019 Jul 25, 62(14), 6694-6704.

13. Fan Yang^#, Kan Wang, Kaixiang Zhou, Bin Dai, Jiapei Dai, Yi Liang^*, Mengchao Cui^*. Synthesis and bioevaluation of technetium-99 m / rhenium labeled phenylquinoxaline derivatives as Tau imaging probes. Eur. J. Med. Chem. 2019 Sep 1, 177, 291-301.

14. Ji-Ying Hu^#, De-Lin Zhang, Xiao-Ling Liu, Xue-Shou Li, Xiao-Qing Cheng, Jie Chen, Hai-Ning Du, Yi Liang^*. Pathological concentration of zinc dramatically accelerates abnormal aggregation of full-length human Tau and thereby significantly increases Tau toxicity in neuronal cells. Biochim. Biophys. Acta-Mol. Basis Dis. 2017 Feb, 1863(2), 414-427.

15. Ting Zhang^#, Jing Li^#, Yong-Zhong Jiang, Jun-Qiang Xu, Xu-Hua Guan, Li-Qiang Wang, Jie Chen, Yi Liang^* (2022). Genotype distribution and evolutionary analysis of rotavirus associated with acute diarrhea outpatients in Hubei, China, 2013–2016. Virol. Sin. 37(4), 503-512.

16. Yuying Li^#, Kan Wang, Kaixiang Zhou, Wentao Guo, Bin Dai, Yi Liang^*, Jiapei Dai, Mengchao Cui^* (2018). Novel D-A-D based near-infrared probes for the detection of beta-amyloid and Tau fibrils in Alzheimer's disease. Chem. Commun. 54(63), 8717-8720.