1998-2002 吉林大學(xué), 生物化學(xué), 學(xué)士
2002-2008 北京大學(xué), 生物化學(xué)與分子生物學(xué), 博士
2008-2013 美國(guó)加州大學(xué)洛杉磯分校 博士后
2013-09 至今, 中國(guó)科學(xué)院上海有機(jī)化學(xué)研究所, 生物與化學(xué)交叉研究中心, 研究員，課題組長(zhǎng)。
劉聰研究員聚焦神經(jīng)退行性疾病中關(guān)鍵致病蛋白質(zhì)的相分離與病理聚集研究。病理性淀粉樣蛋白聚集的結(jié)構(gòu)基礎(chǔ)，包括在各種神經(jīng)退行性疾病（如阿爾茨海默病、帕金森病和肌萎縮側(cè)索硬化癥）中起關(guān)鍵作用的α-syn、Tau、FUS和hnRNPA1；開發(fā)體外和體內(nèi)淀粉樣蛋白結(jié)構(gòu)表征的方法（例如電子衍射、Cryo-ET、細(xì)胞內(nèi)NMR）；研究折疊伴侶與淀粉樣蛋白相互作用背后的分子機(jī)制；基于結(jié)構(gòu)的病理性淀粉樣蛋白聚集抑制劑設(shè)計(jì)；研究在重要生物過(guò)程和病理中涉及的蛋白質(zhì)的液-液相分離結(jié)構(gòu)；設(shè)計(jì)具有應(yīng)用功能的淀粉樣生物材料。
2022年?yáng)|方英才計(jì)劃領(lǐng)軍項(xiàng)目（第十六批上海領(lǐng)軍人才）,
2020年度“上海市優(yōu)秀學(xué)術(shù)帶頭人”
2014 上海市“千人計(jì)劃” 青年項(xiàng)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.?
