Professor | Li Dan | Asia Growth Partners

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Name	Li Dan
Contact Information	lidan2017@sjtu.edu.cn
Language ability	Chinese, English
Province	Shanghai

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Name

Li Dan

Contact Information

lidan2017@sjtu.edu.cn

Language ability

Chinese, English

Province

Shanghai

University/Lab Affiliation and Title	Shanghai Jiao Tong University
Faculty	Bio-X Research Institute
Academic Background & Achievements	1998-2002 Bachelor: Jilin University 2002-2008 Doctorate: Peking University 2008-2013 Postdoctoral: University of California, Los Angeles (UCLA)/Howard Hughes Medical Institute

University/Lab Affiliation and Title

Shanghai Jiao Tong University

Faculty

Bio-X Research Institute

Academic Background & Achievements

1998-2002 Bachelor: Jilin University
2002-2008 Doctorate: Peking University
2008-2013 Postdoctoral: University of California, Los Angeles (UCLA)/Howard Hughes Medical Institute

Areas of Focus	Protein phase separation and phase transition Neurodegenerative diseases
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

Protein phase separation and phase transition
Neurodegenerative diseases

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

Protein Phase Separation Phase Transition Biophysics Biochemistry Cell Biology Neurodegenerative Disease Amyloid Aggregation

Xuechun Xia - Shanghai Jiao Tong University

Chunling Wan - Shanghai Jiao Tong University

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