1998-2002 吉林大学, 生物化学, 学士

2002-2008 北京大学, 生物化学与分子生物学, 博士

2008-2013 美国加州大学洛杉矶分校 博士后

2013-09 至今, 中国科学院上海有机化学研究所, 生物与化学交叉研究中心, 研究员，课题组长。

刘聪研究员聚焦神经退行性疾病中关键致病蛋白质的相分离与病理聚集研究。病理性淀粉样蛋白聚集的结构基础，包括在各种神经退行性疾病（如阿尔茨海默病、帕金森病和肌萎缩侧索硬化症）中起关键作用的α-syn、Tau、FUS和hnRNPA1；开发体外和体内淀粉样蛋白结构表征的方法（例如电子衍射、Cryo-ET、细胞内NMR）；研究折叠伴侣与淀粉样蛋白相互作用背后的分子机制；基于结构的病理性淀粉样蛋白聚集抑制剂设计；研究在重要生物过程和病理中涉及的蛋白质的液-液相分离结构；设计具有应用功能的淀粉样生物材料。

2022年东方英才计划领军项目（第十六批上海领军人才）,

2020年度“上海市优秀学术带头人”

2014 上海市“千人计划” 青年项目

1. Lysophosphatidylcholine binds α-synuclein and prevents its pathological aggregation. Zhao C., Tu J., Wang C., Liu W., Gu J., Yin Y., Zhang S., Li D., Diao J.*, Zhu Z.*, Liu C.*.Natl Sci Rev. 2024 May 25;11(6):nwae182.

2. Structural mechanism for specific binding of chemical compounds to protein amyloid fibril. Tao Y, Xia W, Zhao X, Tang W, Li Y, Tan L, Li D*, Liu C*. Nature Chemical Biology. 2023. doi. 10.1038/s41589-023-01370-x.

3. Rational design of functional amyloid fibrillar assemblies.  Wang X, Zhang S, Zhang J, Wang Y, Jiang X, Tao Y, Li D, Zhong C*, Liu C*. Chem Soc Rev. 2023 Jun 21. doi: 10.1039/d2cs00756h. (Invited review)

4. Conformational Dynamics of an α-Synuclein Fibril upon Receptor Binding Revealed by Insensitive Nuclei Enhanced by Polarization Transfer-Based Solid-State Nuclear Magnetic Resonance and Cryo-Electron Microscopy. Zhang S, Li J, Xu Q, Xia W, Tao Y, Shi C, Li D, Xiang S*, Liu C*. J Am Chem Soc. 2023 Mar 1;145(8):4473-4484.

5. Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments.  Bai Y, Zhang S, Dong H, Liu Y, Liu C*, Zhang X*. Chem Rev. 2023 Nov 8;123(21):12254-12311. (Invited review)

6. Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases. Li D*, Liu C*. Nature Reviewers Neuroscience. 2022 May 30. (Invited review)

7. The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type α-synuclein. Sun Y, Long H, Xia W, Wang K, Zhang X, Sun B, Cao Q, Zhang Y, Dai B, Li D*, Liu C*. Nature Communications. (2021).12(1):6252.

8. Hsp70 chaperones TDP-43 in dynamic, liquid-like phase and prevents it from amyloid aggregation Gu J, Wang C, Hu R, Li Y, Zhang S, Sun Y, Wang Q, Li D, Fang Y*, Liu C*. Cell Research. (2021). 1024-1027.

9. Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's disease. Zhang S, Liu Y, Jia C, Lim Y, Feng G, Xu E., Long H, Kimura Y, Tao Y, Zhao C, Wang C, Liu Z, Hu J, Ma M, Liu Z, Lin J, Li D, Wang R, Dawson V, Dawson T*, Li YM*, Mao X*, Liu C*. Proc. Natl. Acad. Sci. U S A., (2021). 118(26): e2011196118.

10. Wild-type α-synuclein inherits the structure and exacerbated neuropathology of E46K mutant fibril strain by cross-seeding. Long H.F., Zheng W, Liu Y, Sun Y, Zhao K, Liu Z, Xia W, Lv S, Liu Z, Li D, He K*, Liu C.*. Proc. Natl. Acad. Sci. U S A., (2021). 118(20): e2012435118.

11. The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J*, Liu C*. Proc. Natl. Acad. Sci. U S A., (2021). 118(14): e2022933118.

12. Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease. Li D*, Liu C*. Nature Chemical Biology. (2021). 17(3):237-245. (Invited review).

13. Phase separation of protein tyrosine phosphatase underlies MAPK hyperactivation by disease-associated SHP2 mutants. Zhu G, Xie J, Kong W, Xie J, Li Y, Du L, Zheng Q, Sun L, Guan M, Li H, Zhu T, He H, Liu Z, Xia X, Kan C, Tao Y, Shen H, Li D, Wang S, Yu Y, Yu Z, Zhang Z, Liu C*, Zhu J*. Cell. (2020). 183(2):490-502.e18.  

14. Parkinson's disease-related phosphorylation at Tyr39 rearranges α-synuclein amyloid fibril structure revealed by cryo-EM. Zhao K, Lim Y, Liu Z, Long H, Sun Y, Hu J, Zhao C, Tao Y, Zhang X, Li D, Li YM*, Liu C*. Proc Natl Acad Sci U S A. (2020). 117(33): 20305-20315.

15. Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation. Liu Z, Zhang S, Gu J, Tong Y, Li Y, Gui X, Long H, Wang C, Zhao C, Lu J, He L, Li Y, Liu Z, Li D*, Liu C*. Nature Structural & Molecular Biology, (2020). 27(4):363-372.

16. Different regions of synaptic vesicle membrane regulate VAMP2 conformation for the SNARE assembly. Wang C, Tu J, Zhang S, Cai B, Liu Z, Hou S, Zhong Q, Hu X, Liu W, Li G, Liu Z, He L, Diao J, Zhu Z, Li D*, Liu C*. Nature Communications, (2020), 11(1):1531.

17. Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a novel fibril structure. Zhao K, Li Y, Liu Z, Long H, Zhao C, Luo F, Sun Y, Tao Y, Su X, Li D*, Li X*, Liu C*. Nature Communications, (2020). 11(1):2643.

18. Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson's disease familial A53T mutation. Sun Y, Hou S, Zhao K, Long H, Liu Z, Gao J, Zhang Y, Su X, Li D*, Liu C*, Cell Research, 2020, 0, 1-3.

19. Amyloid fibril structure of α-synuclein determined by cryoelectron microscopy. Li Y, Zhao C, Luo F, Liu Z, Gui X, Luo Z, Zhang X, Li D*, Liu C*, Li X* Cell Research, (2018). Sep;28(9):897-903.

20. Atomic structures of two segments from FUS LC domain reveal reversible amyloid fibril formation. Luo F, Gui X, Zhou H, Gu J, Li Y, Liu X, Zhao M, Li D*, Li X.M*, and Liu C*. Nature Structural & Molecular Biology. (2018), 25, 341-346.