2025

1. Wu, K.M., Xu, Q.H., Liu, Y.Q., Feng, Y.W., Han, S.D., Zhang, Y.R., Chen, S.D., Guo, Y., Wu, B.S., Ma, L.Z., Zhang, Y., Chen, Y.L., Yang, L., Yao, Y.F., Xiao, Y.J., Wang, T.T., Zhao, J., Chen, S.F., Cui, M., Lu, B.X., Le, W.D., Shu, Y.S., Ye, K.Q., Li, J.Y., Li, W.S., Wang, J., Liu, C.*, Yuan, P., Yu, J.T. Neuronal FAM171A2 mediates α-synuclein fibril uptake and drives Parkinson’s disease. Science, 2025.

2. Zhang, J.Q.¶, Hu, J.J.¶, Liu, R.G.¶, Zhou, T., Luo, X.W., Liang, P.G., Xie, Z.C., Zhao, Q.Y., Chen, Y., Du, D., Liu, C., Zheng, Y.M., Li, D., Wang, B.* YAP maintains the dynamics of TDP-43 condensates and antagonizes TDP-43 pathological aggregates. Nature Cell Biology, 2025.

3. Zhao, Q.Y., Tao, Y.Q., Yao, Y.X., Liu, K.E., Lv, S.R., Cui, B.Y., Xiao, W.D., Cao, T.Y., Li, W.D., Gao, F., Shen, Y., Wang, C., Ma, C., Qiu, W.Y., Liu, C.*, Li, D. Unraveling Alzheimer’s complexity with a distinct Aβ42 fibril type and specific AV-45 binding. Nature Chemical Biology, 2025.

4. Wang, H.L., Wang, Q., Xu, H.X., Wu, Y.Z., Siulam, C., Xu, Q.H., Pan, C.F., Cao, J.Y., Cao, Z.Y., Yang, R.N., Ding, Y., Fei, Y.Y., Chen, Y.F., Wang, J., Liu, C.*, Lu, B.X. MEK1/2 inhibitors suppress pathological α-synuclein and neurotoxicity in cell models and a humanized mouse model of Parkinson’s disease. Science Translational Medicine, 2025.

5. Wang, Q.W., Liu, Z.T., Wang, Y.J., Liu, Y., Chen, Y., Zhang, S.N., Zeng, W., Li, D., Yang, F., He, Z.H., Xiao, W.D., Liu, C.*, Wang, C. Quantitative chemoproteomics reveals dopamine’s protective modification of Tau. Nature Chemical Biology, 2025.

6. Xia, W.C., Xu, Z.X., Dong, H., Zhang, S.N., He, C.D., Li, D., Sun, B., Dai, B., Dong, S.W., Liu, C.*. Design and Structural Elucidation of Glycopeptide Fibrils: Emulating Glycosaminoglycan Functions for Biomedical Applications. Journal of the American Chemical Society, 2025.

7. Ma, Y.Y.¶, Zhang, Q.Y.¶, Li, D.K., Zhao, K., Li, Z.F., Liu, Y., Wang, C., Sun, B., Li, D., Yuan, J.Y., Liu, C. Intercellular propagation of RIPK1/RIPK3 amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America, 2025.

8. Wei, Q.J.¶, Liu, D.L.¶, Xia, W.C.¶, Wang, F.Z., Lu, H., Zhang, J., Wang, X.Y., Xu, Z.X., He, C.D., Li, W.Z., Shi, X.M., Wang, C., Liu, Y., Liu, C., Dong, S.W.*. An O-glycopeptide participates in the formation of distinct Aβ42 fibril structures and attenuates Aβ42 neurotoxicity. Nature Communications, 2025.

9. Zeng, S.Y.¶, Xiong, X.Y., Long, H.F., Xu, Q.H., Yu, Y.F., Sun, B., Liu, C., Wang, Z.Z., Xu, W.Q., Zhang, S.N., Li, D.*. Design of Ig-like binders targeting α-synuclein fibril for mitigating its pathological activities. Nature Communications, 2025.

10. Cao, T.Y.¶, Zhao, Q.Y.¶, Yao, Y.X., Liu, K.E., Tao, Y.Q., Lv, S.R., Gao, F., Shen, Y., Ma, C., Qiu, W.Y., Liu, C., Le, W.D., Li, D. In situ amplification of α-synuclein amyloid fibril reveals a distinct polymorph related to Parkinson’s disease and dementia with Lewy body. Cell Reports, 2025.

11. Ma, B.Y.¶, Yao, Y.X.¶, Dong, H.¶, Yang, L.L.¶, Li, D.N., Zhao, Q.Y., Sun, B., Chen, Y., Liu, C., Li, D.*. Atomic structure and in situ visualization of native PMEL lamellae in melanosomes. Nature Communications, 2025.

12. Wang, M.J.¶, Xia, W.C.¶, Zhao, D., Zhai, Z.Y., Chen, R.J., Bai, X., Zhang, Z., Fan, H., Zhang, J.P., Liu, C., Jiao, F.. Amyloid Fibrillation of a Ninjurin-1-Derived α-Helical Peptide: Structural Insights into Conformational Transition. ACS Nano, 2025.

13. Zhang, S.N.¶, Liu, K.E.¶, Li, D., Liu, C.. Rising Stars: Molecular Mechanisms and Chemical Interventions of α-Synuclein Amyloid Aggregation in Parkinson’s Disease. Journal of Molecular Biology, 2025.

2024

1. Xu, Q.H., Wang, H.L., Yang, R.N., Tao, Y.Q., Wang, Z.Y., Zhang, S.N., Sun, B., Li, D., Lu, B.X., Liu, C.*. α-Synuclein amyloid fibril directly binds to LC3B and suppresses SQSTM1/p62-mediated selective autophagy. Cell Research, 2024.

2. Zhao, Q.Y., Fan, Y., Zhao, W.B., Ni, Y., Tao, Y.Q., Bian, J., Xia, W.C., Yu, W.B., Fan, Z., Liu, C.*, Sun, B., Le, W.D., Li, W.S., Wang, J., Li, D. A Tau PET tracer PBB3 binds to TMEM106B amyloid fibril in brain. Cell Discovery, 2024.

3. Tao, Y.Q., Xu, P., Zhang, S.Q., Wei, S.G., Yang, G., Liu, K.E., Li, X., Sun, Y.P., Zhao, Q.Y., Li, D., Yu, B., Liu, C.*. Time-course remodeling and pathology intervention of α-synuclein amyloid fibril by heparin and heparin-like oligosaccharides. Nature Structural & Molecular Biology, 2024.

4. Zhang, S.Q., Xiang, H.J., Tao, Y.Q., Li, J., Zeng, S.Y., Xu, Q.H., Xiao, H.N., Lv, S.R., Song, C.W., Cheng, Y., Li, M., Zhu, Z.Y., Zhang, S.N., Sun, B., Li, D., Xiang, S.Q., Tan, L., Liu, C.*. Inhibitor Development for α-Synuclein Fibril’s Disordered Region to Alleviate Parkinson’s Disease Pathology. Journal of the American Chemical Society, 2024.

5. Liu, K.E., Tao, Y.Q., Zhao, Q.Y., Xia, W.C., Li, X., Zhang, S.Q., Yao, Y.X., Xiang, H.J., Han, C., Tan, L., Sun, B., Li, D., Li, A., Liu, C.*. Binding adaptability of chemical ligands to polymorphic α-synuclein amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America, 2024.

6. Zhao, W.B., Liu, K.E., Fan, Y., Zhao, Q.Y., Tao, Y.Q., Zhang, M.W., Gan, L.H., Yu, W.B., Sun, B., Li, D., Liu, C., Wang, J. Cryo-EM structures reveal variant Tau amyloid fibrils between the rTg4510 mouse model and sporadic human tauopathies. Cell Discovery, 2024.

7. Jiang, Y.Q., Gu, J.G., Niu, X.D., Hu, J.J., Zhang, Y.Z., Li, D., Tang, Y.D., Liu, C., Li, Z.J. Phosphorylation-Regulated Dynamic Phase Separation of HIP-55 Protects Against Heart Failure. Circulation, 2024.

8. Hou, S., Hu, J.J., Yu, Z.W., Li, D, Liu, C., Zhang, Y. Machine learning predictor PSPire screens for phase-separating proteins lacking intrinsically disordered regions. Nature Communications, 2024.

2023

1. Bai, Y.L., Zhang, S.N., Dong, H., Liu, Y., Liu, C., Zhang, X. Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments. Chemical Reviews, 2023.

2. Li, D., Liu, C. Molecular rules governing the structural polymorphism of amyloid fibrils in neurodegenerative diseases. Structure, 2023.

3. Lai, Y., Zhao, C.Y., Tian, Z.Q., Wang, C.C.¶, Fan, J.Q.¶, Hu, X., Tu, J., Li, T.H., Leitz, J., Pfuetzne, R.A., Liu, Z.T., Zhang, S.N., Su, Z.M., Burré, J., Li, D., Südhof, T.C., Zhu, Z.J., Liu, C., Brunger, A.T., Diao, J.J.* Neutral lysophosphatidylcholine mediates α-synuclein-induced synaptic vesicle clustering. Proceedings of the National Academy of Sciences of the United States of America, 2023.

4. Li, D.N., Ma, Y.Y., Xia, W.C., Tao, Y.Q., Zhang, Y.L., Zhang, H., Li, D., Dai, B., Liu, C. Creating an Amyloid ‘Kaleidoscope’ Using Short Iodinated Peptides. Angewandte Chemie International Edition, 2023.

5. Wang, F.H., Xia, W.C., Zhang, M.M., Wu, R.R., Song, X.L., Hao, Y., Feng, Y.H., Zhang, L.W., Li, D., Kang, W.Y., Liu, C., Liu, L. Engineering of antimicrobial peptide fibrils with feedback degradation of bacterial-secreted enzymes. Chemical Science, 2023.

6. Wang, X.Y., Zhang, S.N., Zhang, J.C., Wang, Y.M., Jiang, X.Y., Tao, Y.Q., Li, D., Zhong, C., Liu, C. Rational design of functional amyloid fibrillar assemblies. Chemical Society Reviews, 2023.

7. Xiang, J., Tao, Y.Q., Xia, Y.Y., Luo, S.L., Zhao, Q.Y., Li, B.W., Zhang, X.Q., Sun, Y.P., Xia, W.C., Zhang, M.M., Kang, S.S., Ahn, E.H., Liu, X., Xie, F., Guan, Y.H., Yang, J.J., Bu, L.H., Wu, S.X., Wang, X.C., Cao, X.B., Liu, C., Zhang, Z.T., Li, D., Ye, K.Q.* Development of an α-synuclein positron emission tomography tracer for imaging synucleinopathies. Cell, 2023.

8. Tao, Y.Q., Xia, W.C., Zhao, Q.Y., Xiang, H.J., Han, C., Zhang, S.Q., Gu, W., Tang, W.J, Li, Y., Tan, L., Li, D., Liu, C. Structural mechanism for specific binding of chemical compounds to amyloid fibrils. Nature Chemical Biology, 2023.

9. Xu, Q.H., Ma, Y.Y., Sun, Y.P., Li, D., Zhang, X., Liu, C.* Protein amyloid aggregate: Structure and function. Aggregate, 2023.

10. Yang, Z.F., Wang, Y., Wei, M., Li, S., Jia, C.C., Cheng, C., Nusaif, M., Zhang, J., Liu, C., Le, W.D.* Intrastriatal injection of Parkinson’s disease intestine and vagus lysates initiates α-synucleinopathy in rat brain. Cell Death & Disease, 2023.

11. Li, X., Lv, P., Du, Y.F., Xing, C., Liu, C. Emerging roles of O-glycosylation in regulating protein aggregation, phase separation, and functions. Current Opinion in Chemical Biology, 2023.

12. Wang, F.R., Jin, T., Li, H.Y., Long, H.F., Liu, Y., Jin, S., Lu, Y.Y., Peng, Y.H., Liu, C., Zhao, L.H., Wang, X.H. Cannabidivarin alleviates α-synuclein aggregation via DAF-16 in Caenorhabditis elegans. FASEB Journal, 2023.

13. Zhang, S.N., Li, J., Xu, Q.H., Xia, W.C., Tao, Y.Q., Shi, C.W., Li, D., Xiang, S.Q., Liu, C. 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. Journal of the American Chemical Society, 2023.

2022

1. Li, D., Liu, C. Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases. Nature Reviews Neuroscience, 2022.

2. Fan, Y., Zhao, Q.Y., Xia, W.C., Tao, Y.Q., Yu, W.B., Chen, M.J., Liu, Y.Q., Zhao, J., Sun, Y.P., Si, C.F., Zhang, S.Q., Zhang, Y.Y., Li, W.S., Liu, C., Wang, J., Li, D.* Generic amyloid fibrillation of TMEM106B in patient with Parkinson’s disease dementia and normal elders. Cell Research, 2022.

3. Zhu, S.B., Gu, J.G., Yao, J.J., Li, Y.C., Zhang, Z.T., Xia, W.C., Wang, Z., Gui, X.R., Li, L.T., Li, D., Zhang, H., Liu, C. Liquid-liquid phase separation of RBGD2/4 is required for heat stress resistance in Arabidopsis. Developmental Cell, 2022.

4. Lu, S., Hu, J.J., Arogundade, O.A., Goginashvili, A., Vazquez-Sanchez, S., Diedrich, J.K., Gu, J.G., Blum, J., Oung, S., Ye, Q.Z., Yu, H.Y., Ravits, J., Liu, C., Yates, J.R., Cleveland, D.W.* Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition. Nature Cell Biology, 2022.

5. 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 Reports, 2022.

6. Song, Y.X., Dai, B., Wang, Y., Wang, Y., Liu, C., Gourdon, P., Liu, L., Wang, K.T., Dong, M.D.*, Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation. Nano Letters, 2022.

7. Wang, Q., Li, Z.X., Zhang, S.Q., Li, Y.C., Wang, Y., Fang, Z., Ma, Y.N., Liu, Z., Li, D., Liu, C., Ye, M.L., Global profiling of arginine dimethylation in regulating protein phase separation by a steric effect-based chemical-enrichment method. Proceedings of the National Academy of Sciences of the United States of America, 2022.

8. Li, Y.C., Lu, S.Y., Gu, J.G., Xia, W.C., Zhang, S.N., Zhang, S.Q., Wang, Y., Zhang, C., Sun, Y.P., Lei, J., Liu, C., Su, Z.M., Yang, J.T., Peng, X.Z., Li, D., SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation. Protein & Cell, 2022.

9. Fan, Y., Sun, Y.P., Yu, W.B., Tao, Y.Q., Xia, W.C., Liu, Y.Q., Zhao, Y.Q., Tang, Y.L., Sun, Y.M., Liu, F.T., Cao, Q., Wu, J.J., Liu, C., Wang, J., Li, D., Conformational change of α-synuclein fibrils in cerebrospinal fluid from different clinical phases of Parkinson’s disease. Structure, 2022.

10. Li, Y.C., Gu, J.G., Wang, C., Hu, J.J., Zhang, S.Q., Liu, C., Zhang, S.N., Fang, Y.S., Li, D.*, Hsp70 exhibits a liquid-liquid phase separation ability and chaperones condensed FUS against amyloid aggregation. iScience, 2022.

11. Wang, L.Q., Ma, Y.Y., Yuan, H.Y., Zhao, K., Zhang, M.Y., Wang, Q., Huang, X., Dai, B., Chen, J., Li, D., Zhang, D.L., Wang, Z.Z., Zou, L.Y., Yin, P., Liu, C., Liang, Y., Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion. Nature Communications, 2022.

12. Zhao, Q.Y., Tao, Y.Q., Zhao, K., Ma, Y.Y., Xu, Q.H., Liu, C., Zhang, S.N., Li, D.*, Structural insights of Fe³⁺ induced α-synuclein fibrillation in Parkinson's disease. Journal of Molecular Biology, 2022.

13. Gao, C., Gu, J.G., Zhang, H., Jiang, K., Tang, L.L., Liu, R., Zhang, L., Zhang, P.F., Liu, C., Dai, B., Song, H.*, Hyperosmotic-stress-induced liquid-liquid phase separation of ALS-related proteins in the nucleus. Cell Reports, 2022.

14. 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. Nature Communications, 2022.

15. 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.

16. Li, J., Xie, J.F., Godec, A., Weninger, K.R., Liu, C., Smith, J.C., Hong, L.*, Non-ergodicity of a globular protein extending beyond its functional timescale. Chemical Science, 2022.

17. Huang, C.A., Lu, J.X., Ma, X.J., Qiang, J.L., Wang, C.C., Liu, C., Fang, Y.S., Zhang, Y.Y., Li, D., Zhang, S.N., The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins. Journal of Biological Chemistry, 2022.

18. Li, Y.C., Gu, J.G., Liu, C., Li, D., A high-throughput method for exploring the parameter space of protein liquid-liquid phase separation. Cell Reports Physical Science, 2022.

19. Long, H.F., Zeng, S.Y., Sun, Y.P., Liu, C.*, Biochemical and biophysical characterization of pathological aggregation of amyloid proteins. Biophysics Reports, 2022.

2021

1. Liu, D.L., Wei, Q.J., Xia, W.C., He, C.D., Zhang, Q.K., Huang, L., Wang, X.Y., Sun, Y.P., Ma, Y.Y., Zhang, X.H., Wang, Y., Shi, X.M., Liu, C., Dong, S.W., O-Glycosylation Induces Amyloid-β To Form New Fibril Polymorphs Vulnerable for Degradation. Journal of the American Chemical Society, 2021.

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

3. Wang, L.Q., Zhao, K., Yuan, H.Y., Dang, H.B., Ma, Y.Y., Wang, Q., Wang, C., Sun, Y.P., Chen, J., Li, D., Zhang, D.L., Yin, P., Liu, C., Liang, Y., Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM. Science Advances, 2021.

4. Sun, Y.P., Zhang, S.Q., Hu, J.J., Tao, Y.Q., Xia, W.C., Gu, J.G., Li, Y.C., Cao, Q., Li, D., Liu, C.*, Molecular structure of an amyloid fibril formed by FUS low-complexity domain. iScience, 2021.

5. Li, D., Liu, C., Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease. Nature Chemical Biology, 2021.

6. Tao, Y.Q., Xie, J.F., Zhong, Q.L., Wang, Y.Y., Zhang, S.N., Luo, F., Wen, F.C., Xie, J.J., Zhao, J.W., Sun, X.O., Long, H.F., Ma, J.F., Zhang, Q., Long, J.G., Fang, X.Y., Lu, Y., Li, D., Li, M., Zhu, J.D., Sun, B., Li, G.H., Diao, J.J., Liu, C.*, A novel partially-open state of SHP2 points to a "multiple gear" regulation mechanism. Journal of Biological Chemistry, 2021.

7. Wu, X.L., Ma, Y.Y., Zhao, K., Zhang, J., Sun, Y.P., Li, Y.C., Dong, X.Q., Hu, H., Liu, J., Wang, J., Zhang, X., Li, B., Wang, H.Y., Li, D., Sun, B., Lu, J.X., Liu, C., The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. Proceedings of the National Academy of Sciences of the United States of America, 2021.

8. Long, H.F., Zheng, W.T., Liu, Y., Sun, Y.P., Zhao, K., Liu, Z.Y., Xia, W.C., Lv, S.R., Liu, Z.T., Li, D., He, K.W., Liu, C., Wild-type α-synuclein inherits the structure and exacerbated neuropathology of E46K mutant fibril strain by cross-seeding. Proceedings of the National Academy of Sciences of the United States of America, 2021.

9. Zhang, S.N., Liu, Y.Q., Jia, C.Y., Lim, Y.J., Feng, G.Q., Xu, E.Q., Long, H.F., Kimura, Y., Tao, Y.Q., Zhao, C.Y., Wang, C.C., Liu, Z.Y., Hu, J.J., Ma, M.R., Liu, Z.J., Lin, J., Li, D., Wang, R.X., Dawson, V.L., Dawson, T.M., Li, Y.M., Mao, X.B., Liu, C., Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson’s disease. Proceedings of the National Academy of Sciences of the United States of America, 2021.

10. Gu, J.G., Wang, C., Hu, R.F., Li, Y.C., Zhang, S.N., Sun, Y.P., Wang, Q.Q., Li, D., Fang, Y.S., Liu, C., Hsp70 chaperones TDP-43 in dynamic, liquid-like phase and prevents it from amyloid aggregation. Cell Research, 2021.

11. Li, D., Liu, C., Spatiotemporal dynamic regulation of membraneless organelles by chaperone networks. Trends in Cell Biology, 2021.

2020

1. Li, D., Liu, C., Structural diversity of amyloid fibrils and advances in their structure determination. Biochemistry, 2020.

2. Zhao, K., Li, Y., Liu, Z., Long, H., Zhao, C., Luo, F., Sun, Y., Tao, Y., Su, X., Li, D., Li, X.M., Liu, C.*, Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure. Nature Communications, 2020.

3. Zhang, H., Ji, X., Li, P., Liu, C., Lou, J., Wang, Z., Wen, W., Xiao, Y., Zhang, M., Zhu, X., Liquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases. Science China Life Sciences, 2020.

4. Wang, L., Zhao, K., Yuan, H.-Y., Wang, Q., Guan, Z., Tao, J., Li, X., Sun, Y., Yi, C., Chen, J., Li, D., Zhang, D., Yin, P., Liu, C., Liang, Y., Cryo-EM structure of an amyloid fibril formed by full-length human prion protein. Nature Structural & Molecular Biology, 2020.

5. 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, J., Li, D., Liu, C., Different regions of synaptic vesicle membrane regulate VAMP2 conformation for the SNARE assembly. Nature Communications, 2020.

6. Wang, C., Duan, Y., Duan, G., Wang, Q., Zhang, K., Deng, X., Qian, B., Gu, J., Ma, Z., Zhang, S., Guo, L., Liu, C., Fang, Y., Stress induces dynamic, cytotoxicity-antagonizing TDP-43 nuclear bodies via paraspeckle lncRNA NEAT1-mediated liquid-liquid phase separation. Molecular Cell, 2020.

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

8. Liu, Z.Y., Zhang, S.N., Gu, J.G., Tong, Y.L., Li, Y.C., Gui, X.R., Long, H.F., Wang, C.C., Zhao, C.Y., Lu, J.X., He, L., Li, Y., Liu, Z.J., Li, D., Liu, C.*, Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation. Nature Structural & Molecular Biology, 2020.

9. Zhu, G.Y., Xie, J.J., Kong, W.N., Xie, J.F., Li, Y.C., Du, L., Zheng, Q.G., Sun, L., Guan, M.F., Li, H., Zhu, T.X., He, H., Liu, Z.Y., Xia, X., Kan, C., Tao, Y.Q., Shen, H.C., Li, D., Wang, S.Y., Yu, Y.G., Yu, Z.H., Zhang, Z.Y., Liu, C.*, Zhu, J.D., Phase separation of disease-associated SHP2 mutants underlies MAPK hyperactivation. Cell, 2020.