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个人简介

教育经历 1998-2000 中国科学院生物物理研究所,生物化学,博士后 1995-1998 武汉大学,生物物理化学,博士 1985-1988 武汉大学,生物物理化学,硕士 1981-1985 武汉大学,化学,学士 工作经历与任职情况 2013-至今 武汉大学生命科学学院,二级教授、博士生导师。 2001-至今 武汉大学生命科学学院,教授、博士生导师 2013 美国密歇根大学,高级访问学者 2008 美国国立健康研究院(NIH),高级访问学者 2006-2007 美国国立健康研究院(NIH),高级访问学者 2001-2002 法国Louis Pasteur大学,高级访问学者 1996-1998 武汉工程大学,副教授 1988-1995 武汉工程大学,讲师 学术兼职 2014-至今 中国生物化学与分子生物学会理事 2022-至今 中国生物物理学会生物微量元素分会副会长 2015-至今 中国生物物理学会分子生物物理分会理事 2006-至今 《Acta Biochimica et Biophysica Sinica》(SCI源刊)编委 2020-至今 《生命的化学》编委 2013-至今 湖北省生物化学与分子生物学学会副理事长

研究领域

1. 蛋白质结构与功能 2. 疾病的分子基础 3. 信号转导网络中蛋白质相互作用机制及药物筛选

主要开展神经退行性疾病相关重要蛋白质朊蛋白、Tau蛋白、SOD1和TDP-43及其病理突变体淀粉样纤维的冷冻电镜(cryo-EM)结构测定及功能研究,研究这些蛋白质的翻译后修饰、相分离、折叠/错误折叠及其致病机制,研究金属离子、分子伴侣及其翻译后修饰对Tau蛋白液-液相分离、聚集和功能的调控机制,开展以致病蛋白质为靶标的药物设计和新药研发。

近期论文

查看导师最新文章 (温馨提示:请注意重名现象,建议点开原文通过作者单位确认)

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* (2022). Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion. Nature Communications 13(1), 3491. 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* (2021). Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM. Science Advances 7(37), eabg9676. 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* (2020). Cryo-EM structure of an amyloid fibril formed by full-length human prion protein. Nature Structural & Molecular Biology 27(6), 598-602. Ying-Ying Gao#, Tao Zhong#, Li-Qiang Wang, Na Zhang, Yan Zeng, Ji-Ying Hu, Hai-Bin Dang, Jie Chen, Yi Liang* (2022). Zinc enhances liquid-liquid phase separation of Tau protein and aggravates mitochondrial damages in cells. Int. J. Biol. Macromol. 209(Pt A), 703-715. Bin Dai, Tao Zhong, Zhi-Xian Chen, Wang Chen, Na Zhang, Xiao-Ling Liu, Li-Qiang Wang, Jie Chen, Yi Liang* (2021). Myricetin slows liquid-liquid phase separation of Tau and activates ATG5-dependent autophagy to suppress Tau toxicity. J. Biol. Chem. 297(4), 101222. 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* (2020). Phase separation and cytotoxicity of Tau are modulated by protein disulfide isomerase and S-nitrosylation of this molecular chaperone. J. Mol. Biol. 432(7), 2141-2163. 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* (2020). Neutralizing mutations significantly inhibit amyloid formation by human prion protein and decrease its cytotoxicity. J. Mol. Biol. 432(4), 828-844. Kaixiang Zhou, Chang Yuan, Bin Dai, Kan Wang, Yimin Chen, Denglei Ma, Jiapei Dai, Yi Liang*, Hongwei Tan*, Mengchao Cui* (2019). Environment-sensitive near-infrared probe for fluorescent discrimination of Abeta and Tau fibrils in AD brain. J. Med. Chem. 62(14), 6694-6704. Fan Yang, Kan Wang, Kaixiang Zhou, Bin Dai, Jiapei Dai, Yi Liang*, Mengchao Cui* (2019). Synthesis and bioevaluation of technetium-99 m / rhenium labeled phenylquinoxaline derivatives as Tau imaging probes. Eur. J. Med. Chem. 177, 291-301. 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* (2018). Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111. Cell Death Dis. 9(2), 67. 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. Ji-Ying Hu, De-Lin Zhang, Xiao-Ling Liu, Xue-Shou Li, Xiao-Qing Cheng, Jie Chen, Hai-Ning Du, Yi Liang* (2017). 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. 1863(2), 414-427. Haibin Dang, Zhixian Chen, Wang Chen, Xudong Luo, Pan Liu, Liqiang Wang, Jie Chen, Xuhai Tang, Zhengzhi Wang, Yi Liang* (2022). The residues 4 to 6 at the N-terminus in particular modulate fibril propagation of b2-microglobulin. Acta Biochim. Biophys.Sin. 54(2), 187-198. Xu-Dong Luo, Fan-Lou Kong, Hai-Bin Dang, Jie Chen, Yi Liang* (2016). Macromolecular crowding favors the fibrillization of beta2-microglobulin by accelerating the nucleation step and inhibiting fibril disassembly. Biochim. Biophys. Acta 1864(11), 1609-1619. Xiao-Ling Liu, Ji-Ying Hu, Meng-Yun Hu, Yi Zhang, Zheng-Yuan Hong, Xiao-Qing Cheng, Jie Chen, Dai-Wen Pang, Yi Liang* (2015). Sequence-dependent abnormal aggregation of human Tau fragment in an inducible cell model. Biochim. Biophys. Acta-Mol. Basis Dis. 1852(8), 1561-1573. Kai Pan, Chuan-Wei Yi, Jie Chen, Yi Liang* (2015). Zinc significantly changes the aggregation pathway and the conformation of aggregates of human prion protein. Biochim. Biophys. Acta 1854(8), 907-918. Qian Ma, Ji-Ying Hu, Jie Chen, Yi Liang* (2013). The role of crowded physiological environments in prion and prion-like protein aggregation. Int. J. Mol. Sci. 14(11), 21414-21427. Chuan-Wei Yi, Wen-Chang Xu, Jie Chen, Yi Liang* (2013). Recent progress in prion and prion-like protein aggregation. Acta Biochim. Biophys. Sin. 45(6). 520-526. De-Lin Zhang, Ling-Jia Wu, Jie Chen, Yi Liang* (2012). Effects of macromolecular crowding on the structural stability of human alpha-lactalbumin. Acta Biochim. Biophys. Sin. 44(8), 703-711. Zheng Zhou, Jun-Ming Liao, Peng Zhang, Jun-Bao Fan, Jie Chen, Yi Liang* (2011). Parkinson disease drug screening based on the interaction between D2 dopamine receptor and beta-arrestin 2 detected by capillary zone electrophoresis. Protein Cell 2(11), 899-905.

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