超快科学中心

李 丹

  • 教授、长聘副教授

  • 电子邮箱: lidan2017@sjtu.edu.cn

  • 教育背景

  • 工作经历

  • 研究方向

  • 代表性论文和著作

  • 1998.9-2002.7 吉林大学 生命科学学院 学士学位

  • 2002.9-2008.7 北京大学 生命科学学院 博士学位

  • 2008.9-2013.12 加州大学洛杉矶分校 /霍华德休斯医学院 博士后

  • 2014.5-2016.8 中国科学院有机化学研究所 生物与化学交叉中心 学术交流

  • 2017.4-2021.12 上海交通大学 长聘教轨副教授

  • 2022.1-至今 上海交通大学 长聘副教授

  • 2022.8-至今 上海交通大学 教授

  • 神经退行性疾病相关蛋白质相分离和聚集

  • 神经退行性疾病早期诊断探针研发

  1. Long H.F., Zhang S.N., Zeng S.Y., Tong Y.L., Liu J., Liu C.*, Li D.* Interaction of RAGE with α-synuclein fibrils mediates inflammatory response of microglia.Cell Rep, 2022 Sep 20;40(12):111401.

  2. Zhang S.N., Zhu Y., Lu J.X., Liu Z.Y., Lobato A.G., Zeng W., Liu J.Q., Zeng S.Y., Liu C., Liu J., He Z.H., Zhai R.G.*, Li D.* Specific binding of Hsp27 and phosphorylated Tau mitigates abnormal Tau aggregation-induced pathology. Elife. 2022 Sep 1;11:e79898

  3. Tao Y.Q., Sun Y.P., Lv S.R., Xia W.C., Zhao K., Xu Q.H., Zhao Q.Y., He L., Wang Y., Liu C.*, Li D.* Heparin induces α-synuclein to form new fibril polymorphs with attenuated neuropathology. Nat Commun. 2022 Jul 22;13(1):4226.

  4. Zhao Q, Tao Y, Zhao K, Ma Y, Xu Q, Liu C, Zhang S, Li D. Structural Insights of Fe3+ Induced α-synuclein Fibrillation in Parkinson's Disease. J Mol Biol. 2022 Jun 8:167680. doi: 10.1016/j.jmb.2022.167680. Online ahead of print.

  5. Li D*, Liu C.* Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases. Nat Rev Neurosci. 2022 May 30. doi: 10.1038/s41583-022-00603-7. Online ahead of print.

  6. Li Y, Lu S, Gu J, Xia W, Zhang S, Zhang S, Wang Y, Zhang C, Sun Y, Lei J, Liu C, Su Z*, Yang J*, Peng X*, Li D.* SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation. Protein & Cell. 2022 Aug;13(8):602-614. doi: 10.1007/s13238-022-00905-7. Epub 2022 Apr 6.

  7. Fan Y, Zhao Q, Xia W, Tao Y, Yu W, Chen M, Liu Y, Zhao J, Shen Y, Sun Y, Si C, Zhang S, Zhang Y, Li W, Liu C, Wang J*, Li D*. Generic amyloid fibrillation of TMEM106B in patient with Parkinson's disease dementia and normal elders. Cell Res. 2022 Jun;32(6):585-588. doi: 10.1038/s41422-022-00665-3. Epub 2022 Apr 27.

  8. Huang C, Lu J, Ma X, Qiang J, Wang C, Liu C, Fang Y, Zhang Y, Jiang L, Li D*, Zhang S.* The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins. J Biol Chem. 2022 May;298(5):101912. doi: 10.1016/j.jbc.2022.101912. Epub 2022 Apr 7.

  9. Li Y, Gu J, Wang C, Hu J, Zhang S, Liu C, Zhang S, Fang Y, Li D. Hsp70 exhibits a liquid-liquid phase separation ability and chaperones condensed FUS against amyloid aggregation. iScience. 2022 May 5;25(6):104356. doi: 10.1016/j.isci.2022.104356. eCollection 2022 Jun 17.

  10. Li, Y., Gu, J., Liu, C.*, Li, D.* A high-throughput method for exploring the parameter space of protein liquid-liquid phase separation, Cell Reports Physical Science, Volume 3, Issue 3, 16 March 2022, 100764

  11. D. Li* and C. Liu*, Spatiotemporal dynamic regulation of membraneless organelles by chaperone networks, Trends in Cell Biology, 2022 Jan;32(1):1-3

  12. Dan Li* and Cong Liu*, Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease, Nature Chemical Biology, 2021 Mar;17(3):237-245doi: 10.1038/s41589-020-00708-z

  13. Yunpeng Sun#, Kun Zhao#, Wencheng Xia, Jinge Gu, Yeyang Ma, Xinrui Gui, Xia Zhang, Yanshan Fang, Bo Sun, Cong Liu*, Dan Li* The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure, Nature Communications, 2020, Dec 11;11(1):6349. doi: 10.1038/s41467-020-20227-8.

  14. Jinge Gu , Zhenying Liu , Shengnan Zhang , Yichen Li , Wencheng Xia , Chen Wang , Huaijiang Xiang , Zhijun Liu , Li Tan , Yanshan Fang , Cong Liu* , Dan Li*,  Hsp40 proteins phase separate to chaperone the assembly and maintenance of membraneless organelles, PNAS, 2020, Dec 8;117(49):31123-31133 doi: 10.1073/pnas.2002437117.

  15. Zhao, K. , Li, Y., Liu, Z., Long, H., Zhao, C., Luo, F., Sun, Y., Tao, Y., Su, X.-D., Li, D.*, Li, X.*, Liu, C.*, Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure. Nature Communications, 2020 May 26;11(1):2643.

  16. Lu J, Zhang S, Ma X, Jia C, Liu Z, Huang C, Liu C*, Li D.* Structural basis of the interplay between α-synuclein and Tau in regulating pathological amyloid aggregation. J. Biol. Chem. 2020 May 22;295(21):7470-7480. doi: 10.1074/jbc.RA119.012284.

  17. Ma X, Zhu Y, Lu J, Xie J, Li C, Shin WS, Qiang J, Liu J, Dou S, Xiao Y, Wang C, Jia C, Long H, Yang J, Fang Y, Jiang L, Zhang Y, Zhang S, Zhai RG*, Liu C*, Li D* Nicotinamide mononucleotide adenylyltransferase uses its NAD+ substrate-binding site to chaperone phosphorylated Tau. Elife. 2020 Apr 6;9. pii: e51859. doi: 10.7554/eLife.51859.

  18. Sun, Y., Hou, S., Zhao, K., Long, H., Liu, Z., Gao, J., Zhang, Y., Su, X. D., Li, D.*, Liu, C.*. Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson’s disease familial A53T mutation, Cell Research, 2020 Apr;30(4):360-362. doi: 10.1038/s41422-020-0299-4.

  19. Liu, Z., Zhang S., Gu, J., Tong, Y., Li, Y., Gui, X., Long, H., Wang, C., Zhao, C., Lu, J., Lin, H., Li, Y., Liu, Z., Li, D.*, Liu, C.*, Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation. Nature Structural and Molecular Biology. 2020 Apr;27(4):363-372. doi: 10.1038/s41594-020-0399-3.

  20. 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. J., Li, D.*, Liu, C.*, Different regions of synaptic vesicle membrane regulate VAMP2 conformation for the SNARE assembly. Nature Communications. 2020 Mar 24;11(1):1531. doi: 10.1038/s41467-020-15270-4.

  21. Li, D.*, Liu, C.*, Structural Diversity of Amyloid Fibrils and Advances in Their Structure Determination. Biochemistry, 2020 Feb 11;59(5):639-646. doi: 10.1021/acs.biochem.9b01069.

  22. Gui, X., Luo, F., Li, YC, Zhou, H., Qin, Z., Liu, ZY, Gu, JG, Xie, MY, Zhao, K., Dai, B., Shin, WS, He, JH, He, L., Jiang, L., Zhao, ML, Sun, B., Li, XM, Liu, C.*, Li, D.* Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly, Nature Communications, 2019 May 1;10(1):2006.

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

  24. Li, D.*, Liu, C.* Better together: a hybrid amyloid signals necroptosis. Cell 2018 Volume 173, Issue 5, p1068–1070, 17 May.

  25. Luo, F., Gui, X., Zhou, H., Gu, J., Li, Y., Liu, X., Zhao, M., Li, D.*, Li, X.*, Liu, C.*. Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation. Nature Struct. Mol. Biol. 2018 Apr;25(4):341-346