Professor | 李丹 | 数字化转型顾问

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Name	李丹
Contact Information	lidan2017@sjtu.edu.cn
Language ability	中文, 英文
Province	上海

Upload Avatar (500 x 500)

Name

李丹

Contact Information

lidan2017@sjtu.edu.cn

Language ability

中文, 英文

Province

上海

University/Lab Affiliation and Title	上海交通大学
Faculty	Bio-X Research Institute
Academic Background & Achievements	1998-2002 学士: 吉林大学 2002-2008 博士: 北京大学 2008-2013 博士后: 加州大学洛杉矶分校(UCLA)/霍华德休斯医学院

University/Lab Affiliation and Title

上海交通大学

Faculty

Bio-X Research Institute

Academic Background & Achievements

1998-2002 学士: 吉林大学
2002-2008 博士: 北京大学
2008-2013 博士后: 加州大学洛杉矶分校(UCLA)/霍华德休斯医学院

Areas of Focus	蛋白相分离和相变神经退行性疾病
Publications	Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure., 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., 2020 Structural basis of the interplay between α-synuclein and Tau in regulating pathological amyloid aggregation., Lu J, Zhang S, Ma X, Jia C, Liu Z, Huang C, Liu C, Li D., 2020 Nicotinamide mononucleotide adenylyltransferase uses its NAD+ substrate-binding site to chaperone phosphorylated Tau., 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., 2020 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. D., Li, D., Liu, C., 2020 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. J., Li, D., Liu, C., 2020 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., Lin, H., Li, Y., Liu, Z., Li, D., Liu, C., 2020 Structural Diversity of Amyloid Fibrils and Advances in Their Structure Determination., Li, D., Liu, C., 2020 Different heat shock proteins bind α-synuclein with distinct mechanisms and synergistically prevent its amyloid aggregation., Jia, C., Ma, X., Liu, Z., Gu, J., Zhang, X., Li, D., Zhang, S., 2019 Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly., 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., 2019 Structure-Based Peptide Inhibitor Design of Amyloid-b Aggregation., Lu, J., Cao, Q., Wang, C., Zheng, J., Luo, F., Xie, J., Li, Y., Ma, X., He, L., Eisenberg, D., Nowick, J., Jiang, L., Li, D., 2019 Amyloid fibril structure of alpha-synuclein determined by cryo-electron microscopy., Li, Y., Zhao, C., Luo, F., Liu, Z., Gui, X., Luo, Z., Zhang, X., Li, D., Liu, C., Li, X., 2018 Better together: a hybrid amyloid signals necroptosis., Li, D., Liu, C., 2018 Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation., Luo, F., Gui, X., Zhou, H., Gu, J., Li, Y., Liu, X., Zhao, M., Li, D., Li, X., Liu, C., 2018

Areas of Focus

蛋白相分离和相变
神经退行性疾病

Publications

Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure., 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., 2020
Structural basis of the interplay between α-synuclein and Tau in regulating pathological amyloid aggregation., Lu J, Zhang S, Ma X, Jia C, Liu Z, Huang C, Liu C, Li D., 2020
Nicotinamide mononucleotide adenylyltransferase uses its NAD+ substrate-binding site to chaperone phosphorylated Tau., 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., 2020
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. D., Li, D., Liu, C., 2020
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. J., Li, D., Liu, C., 2020
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., Lin, H., Li, Y., Liu, Z., Li, D., Liu, C., 2020
Structural Diversity of Amyloid Fibrils and Advances in Their Structure Determination., Li, D., Liu, C., 2020
Different heat shock proteins bind α-synuclein with distinct mechanisms and synergistically prevent its amyloid aggregation., Jia, C., Ma, X., Liu, Z., Gu, J., Zhang, X., Li, D., Zhang, S., 2019
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly., 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., 2019
Structure-Based Peptide Inhibitor Design of Amyloid-b Aggregation., Lu, J., Cao, Q., Wang, C., Zheng, J., Luo, F., Xie, J., Li, Y., Ma, X., He, L., Eisenberg, D., Nowick, J., Jiang, L., Li, D., 2019
Amyloid fibril structure of alpha-synuclein determined by cryo-electron microscopy., Li, Y., Zhao, C., Luo, F., Liu, Z., Gui, X., Luo, Z., Zhang, X., Li, D., Liu, C., Li, X., 2018
Better together: a hybrid amyloid signals necroptosis., Li, D., Liu, C., 2018
Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation., Luo, F., Gui, X., Zhou, H., Gu, J., Li, Y., Liu, X., Zhao, M., Li, D., Li, X., Liu, C., 2018

蛋白相分离相变生物物理生物化学细胞生物学神经退行性疾病淀粉样聚集

夏学春 - 上海交通大学

万春玲 - 上海交通大学

陆青 - 上海交通大学

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