Significant Works

2023

1. Zhang H., Gu J.G., Zhang Y.L., Guo H.Z., Zhang S.N., Song J., Liu C., Wang L.*, Li D.*, Dai B.*, Graphene Quantum Dots Modulate Stress Granule Assembly and Prevent Abnormal Phase Transition of Fused in Sarcoma Protein. ACS Nano., 2023.

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

3. 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 Dis., 2023.

4. Li X., Lv P., Du Y.F., Xing C.*, Liu C.*, Emerging roles of O-glycosylation in regulating protein aggregation, phase separation, and functions. Curr Opin Chem Biol., 2023.

5. 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 J., 2023.

6. 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. J Am Chem Soc., 2023.

7. Wang Y., Ling X.B., Zhang C., Zou J., Luo B.N., Luo Y.B., Jia X.Y., Jia G.W., Zhang M.H., Hu J.C., Liu T., Wang Y.F.Y., Lu K.F., Li D., Ma J.B.*, Liu C.*, Su Z.M.*, Modular characterization of SARS-CoV-2 nucleocapsid protein domain functions in nucleocapsid-like assembly. Mol Biomed., 2023.

2022

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

2. 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.

3. 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.

4. 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.

5. Zhang S.Q., Dong H., Bian J., Li D., Liu C.*, Targeting amyloid proteins for clinical diagnosis of neurodegenerative diseases. Fundamental Research., 2022.

6. Li X., Zhang S.Q., Liu Z.T., Tao Y.Q., Xia W.C., Sun Y.P., Liu C., Le W.D., Sun B., Li D.*, Subtle change of fibrillation condition leads to substantial alteration of recombinant Tau fibril structure. iScience., 2022.

7. 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. J Biol Chem., 2022.

8. He H., Yang W., Su N., Zhang C.K., Dai J.N., Han F., Singhai M., Bai W.J., Zhu X.L., Zhu J., Liu Z., Xia W.C., Liu X.T., Zhang C.H., Jiang K., Huang W.H., Chen D., Wang Z.Y., He X.Y., Kirchhoff F., Li Z.Y., Liu C., Huan J.N., Wang X.H., Wei W., Wang J.,Augustin H.G., Hu J.H.*, Activating NO-sGC crosstalk in the mouse vascular niche promotes vascular integrity and mitigates acute lung injury. J Exp Med., 2023.

9. Li Y.C., Gu J.G., Liu C., Li D.*, A High-Throughput Method to Profile Protein Liquid-Liquid Phase Separation. Methods in Molecular Biology., 2022.

10. 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 Lett., 2022.

11. Li D.*, Liu C.*, Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases. Nat Rev Neurosci., 2022.

12. 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. Proc. Natl. Acad. Sci. U S A., 2022.

13. 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.

14. 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.

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

16. 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, 25(6).

17. 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, 13(1).

18. Zhao Q.Y., Tao Y.Q., Zhao K., Ma Y.Y., Xu Q.H., Liu C., Zhang S.N., Li D.*, Structural insights of Fe 3+ induced α-synuclein fibrillation in Parkinson's disease. Journal Molecular Biology, 2022.

19. 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, 40(3).

20. 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, 13(1).

21. Guo J.L., Zhao Y.L., Zhang Q., Feng Y., Zhang X., Wang T., Liu C., Ma H.H., Sun B.*, Stochastically multimerized ParB orchestrates DNA assembly as unveiled by single-molecule analysis. Nucleic Acids Research, 2022, 50(16).

22. Teng W., Hu J.J., Li Y.N., Bi L.L., Guo X.S., Zhang X., Li D., Hou X.M., Modesti M., Xi X.G., Liu C.*, Sun B.*, Bloom Syndrome Helicase Compresses Single‐Stranded DNA into Phase‐Separated Condensates. Angewandte Chemie, 2022, 61(39).

23. 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.

24. 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, 24(9).

25. 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, 13(33).

26. 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, 40(12).

27. Li, D.*, Liu, C.*, Spatiotemporal dynamic regulation of membraneless organelles by chaperone networks. Trends in Cell Biology, 2021, 32(1).

28. 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.

29. 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, 298(5).

30. 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, 1-13.

31. 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.

32. 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, 57(5).

33. 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, 22(9).

34. Long, H.F., Zeng, S.Y., Sun, Y.P., Liu, C.*, Biochemical and biophysical characterization of pathological aggregation of amyloid proteins. Biophysics Reports, 2022, 8(1).

35. Long, H.F., Zeng, S.Y., Li, D.*, Cellular and animal models to investigate pathogenesis of amyloid aggregation in neurodegenerative diseases. Biophysics Reports, 2022, 8(1).

36.Li, D.*, Liu, C.*, Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases. Nature Reviews Neuroscience, 2022, 23(9).

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, 143(48).

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, 12(1).

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, 7(37).

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, 25(1).

5. Li, D.*; Liu, C.*, Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease. Nature Chemical Biology, 2021, 17(3), 237-245.

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, 296, 100538.

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, 118(14).

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, 118(20).

9. Zhang, S.N.; Liu, Y.Q.; Jia, C.Y.; Lim, Y.J.; Feng, G.Q.; Xu, E.Q.; Long, H.F.; Yasuyoshi Kimura; 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.; Valina L Dawson; Ted M Dawson*; 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, 118(26).

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.

2020

1.    Li, D.*; Liu, C.* , Structural diversity of amyloid fibrils and advances intheir structure determination. Biochemistry 2020, 59(5), 639-646.

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’sdisease associated mutation E46K of α-synuclein triggers the formation of adistinct fibril structure. Nature communications 2020, 11(1), 1-9.

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, 63 (7), 953-985.

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.; LiuC.*; Liang Y.*, Cryo-EM structure of an amyloid fibril formed by full-lengthhuman prion protein. Nature Structural & Molecular Biology 2020, 1-5.

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 VAMP2conformation for the SNARE assembly. Nature communications 2020, 11(1), 1-12.

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 viaparaspeckle lncRNA NEAT1-mediated liquid-liquid phase separation. MolecularCell 2020,443-458.

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 withParkinson’s disease familial A53T mutation.Cell Research 2020, 30(4), 360-362.

8.    Ma, X.; Zhu, Y.; Lu, J.; Xie, J.; Li, C.; Shin,W. S.; Qiang, J.; Liu, J.; Dou, S.; Xiao; Y.; Xiao Y.; Wang C.; Jia C.; Long H.;Yang J.; Fang Y.; Jiang L.;Zhang Y.; Zhang S.; Zhai R.*; Liu C.*; Li D.*; Nicotinamidemononucleotide adenylyltransferase uses its NAD+ substrate-binding site tochaperone phosphorylated Tau. Elife 2020, 9, e51859.

9.    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 regulatingpathological amyloid aggregation. Journal of Biological Chemistry 2020, 295 (21), 7470-7480.

10.   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.J.; Li D.*;Liu C.*, Hsp27 chaperones FUS phase separation under the modulation ofstress-induced phosphorylation. Nature Structural & Molecular Biology 2020, 27 (4), 363-372.

11.   Zhao, K.; Lim, Y. J.; Liu, Z.; Long, H.; Sun,Y.; Hu, J. J.; Zhao, C.; Tao, Y.; Zhang, X.; Li, D.; Li, Y. M.*; Liu, C.* ,Parkinson's disease-related phosphorylation at Tyr39 rearranges α-synucleinamyloid fibril structure revealed by cryo-EM. Proceedings of the NationalAcademy of Sciences of the United States of America 2020.

12.   Zhu,G. et al. Phase separation ofdisease-associated SHP2 mutants underlies MAPK hyperactivation. Cell 183, 490-502 (2020).

13.   Gu, J. et al. Hsp40 proteins phase separate to chaperone the assembly andmaintenance of membraneless organelles. Proceedingsof the National Academy of Sciences 117, 31123-31133 (2020).

14.   Sun,Y. et al. The nuclear localizationsequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEMstructure. Nature communications 11, 1-8 (2020).

2019

1.   Zhou, H.; Luo, F.; Luo, Z.; Li, D.; Liu, C.* ; Li, X.*, Programmingconventional electron microscopes for solving ultrahigh-resolution structuresof small and macro-molecules. Analytical chemistry 2019, 91(17), 10996-11003.

2.   Zhang, X.; Zhang, S.; Zhang, L.; Lu, J.; Zhao,C.; Luo, F.; Li, D.; Li, X.*; Liu, C.* ,Heat shock protein 104 (HSP104) chaperones soluble Tau via a mechanism distinctfrom its disaggregase activity. Journal of Biological Chemistry 2019, 294 (13), 4956-4965.

3.   Yu, J.; Liu, Z.; Liang, Y.; Luo, F.; Zhang,J.; Tian, C.; Motzik, A.; Zheng, M.; Kang, J.; Zhong, G.; Liu C.; Fang P.; GuoM.; Razin E.*; Wang J.*, Second messenger Ap 4 A polymerizes target proteinHINT1 to transduce signals in FcεRI-activated mast cells. Nature communications 2019, 10 (1), 1-12.

4.   Ma, D. F.; Xu, C. H.; Hou, W. Q.; Zhao, C.Y.; Ma, J. B.; Huang, X.; Jia, Q.; Ma, L.; Diao, J.; Liu, C.* ; Li, M.*; Lu, Y.*, Detecting Single‐Molecule Dynamics on Lipid Membraneswith Quenchers‐in‐a‐LiposomeFRET. Angewandte Chemie 2019,131 (17), 5633-5637.

5.   Lu, J.; Cao, Q.; Wang, C.; Zheng, J.; Luo,F.; Xie, J.; Li, Y.; Ma, X.; He, L.; Eisenberg, D. ; Nowick J. ; Jiang L.* ; LiD.*, Structure-based peptide inhibitor design of amyloid-β aggregation. Frontiersin molecular neuroscience 2019,12, 54.

6.   Liu,C.* ; Fang, Y.*, New insights of poly (ADP-ribosylation) inneurodegenerative diseases: A focus on protein phase separation and pathologicaggregation. Biochemical pharmacology 2019, 167, 58-63.

7.   Jia, C.; Ma, X.; Liu, Z.; Gu, J.; Zhang, X.; Li,D.*; Zhang, S.*, Different heat shock proteins bind α-synuclein with distinctmechanisms and synergistically prevent its amyloid aggregation. Frontiersin neuroscience 2019, 13, 1124.

8.   Gui, X.; Luo, F.; Li, Y.; Zhou, H.; Qin, Z.; Liu,Z.; Gu, J.; Xie, M.; Zhao, K.; Dai, B.; Shin W.; He J.; He L.; JiangL.; Zhao M.; Sun B.; Li X.; Liu C.*; Li D.*, Structural basis for reversibleamyloids of hnRNPA1 elucidates their role in stress granule assembly. Naturecommunications 2019, 10 (1), 1-12.

9.   Duan, Y.; Du, A.; Gu, J.; Duan, G.; Wang, C.;Gui, X.; Ma, Z.; Qian, B.; Deng, X.; Zhang, K.; Sun, L.; Tian, K.; Zhang, Y.; Jiang,H.; Liu, C.* ; Fang, Y.*, PARylationregulates stress granule dynamics, phase separation, and neurotoxicity ofdisease-related RNA-binding proteins. Cell Research 2019, 29(3), 233-247.

10.   Dai, B.; Sargent, C. J.; Gui, X.; Liu, C.;Zhang, F.*, Fibril Self-Assembly of Amyloid–Spider Silk Block Polypeptides. Biomacromolecules 2019, 20 (5), 2015-2023.

11.   Cui, M.; Wang, X.; An, B.; Zhang, C.; Gui,X.; Li, K.; Li, Y.; Ge, P.; Zhang, J.; Liu, C.; Zhang C.*, Exploiting mammalianlow-complexity domains for liquid-liquid phase separation–driven underwateradhesive coatings. Science advances 2019,5 (8), eaax3155.

12.   Cui, M.; Qi, Q.; Gurry, T.; Zhao, T.; An, B.;Pu, J.; Gui, X.; Cheng, A. A.; Zhang, S.; Xun; D.; Becce M.; Briatico F.; Liu C.;Lu T.; Zhong C.*, Modular genetic design of multi-domain functional amyloids:Insights into self-assembly and functional properties. Chemical science 2019, 10(14), 4004-4014.

2018

1.   Zhang, S.; Wang, C.; Lu, J.; Ma, X.; Liu, Z.;Li, D.; Liu, Z.; Liu, C.*  , In-cell NMR study of Tau and MARK2phosphorylated tau. International Journal of Molecular Sciences 2018, 20(1), 90.

2.   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 domainsegments reveal bases for reversible amyloid fibril formation. Naturestructural & molecular biology 2018, 25 (4), 341-346.

3.   Liu, Z.; Wang, C.; Li, Y.; Zhao, C.; Li, T.; Li,D.; Zhang, S.*; Liu, C.* ,Mechanistic insights into the switch of αB-crystallin chaperone activity and self-multimerization. Journalof Biological Chemistry 2018,293 (38), 14880-14890.

4.   Li, Y.; Zhao, C.; Luo, F.; Liu, Z.; Gui, X.; Luo,Z.; Zhang, X.; Li, D.; Liu, C.* ;Li, X.*, Amyloid fibril structure of α-synuclein determined by cryo-electronmicroscopy. Cell research 2018, 28 (9), 897-903.

5.   Li, D.*; Liu,C.* , Better together: a hybrid amyloid signals necroptosis. Cell 2018, 173 (5), 1068-1070.

2017

1.   Liu, Z.; Zhang, S.; Li, D.; Liu, C.*  , A structural view of αB-crystallinassembly and amyloid aggregation. Protein and Peptide Letters 2017, 24(4), 315-321.

2.   Bu, B.; Tong, X.; Li, D.; Hu, Y.; He, W.; Zhao,C.; Hu, R.; Li, X.; Shao, Y.; Liu, C.; Zhao, Q.*; Ji, B.*; Diao, J.*,N-Terminal Acetylation Preserves α-Synuclein from Oligomerization by BlockingIntermolecular Hydrogen Bonds. ACS Chemical Neuroscience 2017, 8(10), 2145-2151.

3.   An, B.; Wang, X.; Cui, M.; Gui, X.; Mao, X.; Liu,Y.; Li, K.; Chu, C.; Pu, J.; Ren, S.; Wang, Y.; Zhong, G.; Lu, T. K.; Liu, C.;Zhong, C.*, Diverse Supramolecular Nanofiber Networks Assembled by FunctionalLow-Complexity Domains. ACS Nano 2017, 11 (7), 6985-6995.

4.   Xie, J.; Si, X.; Gu, S.; Wang, M.; Shen, J.; Li,H.; Shen, J.; Li, D.; Fang, Y.; Liu, C.* , Allosteric inhibitors of SHP2 withtherapeutic potential for cancer treatment.Journal of Medicinal Chemistry 2017, 60 (24), 10205-10219.

2016

1.   Wang, C.; Zhao, C.; Li, D.; Tian, Z.; Lai,Y.; Diao, J.*; Liu, C.* , Versatile structures of α-synuclein. Frontiersin molecular neuroscience 2016,9, 48.

2.   Yang, G.; Zhang, X.; Kochovski, Z.; Zhang,Y.; Dai, B.; Sakai, F.; Jiang, L.; Lu, Y.; Ballauff, M.; Li, X.; Liu, C.* ;Chen, G.*; Jiang, M., Precise and Reversible Protein-Microtubule-Like Structurewith Helicity Driven by Dual Supramolecular Interactions. Journal of the AmericanChemical Society 2016, 138 (6), 1932-1937..

2015

1.   Dai, B.; Li, D.; Xi, W.; Luo, F.; Zhang, X.; Zou,M.; Cao, M.; Hu, J.; Wang, W.; Wei, G.*; Zhang, Y.*; Liu, C.* , Tunableassembly of amyloid-forming peptides into nanosheets as a retrovirus carrier. Proceedingsof the National Academy of Sciences 2015, 112 (10), 2996.

2014

1.   Hochberg, G. K. A.; Ecroyd, H.; Liu, C.; Cox,D.; Cascio, D.; Sawaya, M. R.; Collier, M. P.; Stroud, J.; Carver, J. A.; Baldwin,A. J.; Robinson, C. V.; Eisenberg, D.; Benesch, J. L. P.*;Laganowsky, A.*, The structured core domain ofαB-crystallin can prevent amyloid fibrillation and associated toxicity. Proceedingsof the National Academy of Sciences 2014, 111 (16), E1562.

2.   Li, D.; Jones, E. M.; Sawaya, M. R.; Furukawa,H.; Luo, F.; Ivanova, M.; Sievers, S. A.; Wang, W.; Yaghi, O. M.; Liu, C.;Eisenberg, D.*, Structure-Based Design of Functional Amyloid Materials. Journalof the American Chemical Society 2014, 136 (52), 18044-18051.

3.   Li, D.; Furukawa, H.; Deng, H.; Liu, C.; Yaghi,O. M.*; Eisenberg, D.*, Designed amyloid fibers as materials for selectivecarbon dioxide capture. Proceedings of the National Academy of Sciences 2014, 111 (1), 191.

4.   Gu, L.; Liu, C.; Stroud, J. C.; Ngo, S.; Jiang,L.; Guo, Z.*, Antiparallel triple-strand architecture for prefibrillar Aβ42oligomers. Journal of Biological Chemistry 2014, 289 (39), 27300-27313.

2013

1.   Jiang, L.; Liu, C.; Leibly, D.; Landau, M.; Zhao,M.; Hughes, M. P.; Eisenberg, D.*, Structure-based discovery of fiber-bindingcompounds that reduce the cytotoxicity of amyloid beta. Elife 2013, 2,e00857.

2.   Gu, L.; Liu, C.; Guo, Z.*, Structuralinsights into Aβ42 oligomers using site-directed spin labeling. Journal of Biological Chemistry 2013,288 (26), 18673-18683.

2012

1.   Stroud, J. C.; Liu, C.; Teng, P.; Eisenberg,D.*, Toxic fibrillar oligomers of amyloid-β have cross-β structure. Proceedings of the National Academy of Sciences 2012, 109 (20), 7717-7722.

2.   Li, D.; Fu, T.; Nan, J.; Liu, C.; Li, L.; Su,X.*, Structural basis for the autoinhibition of the C-terminal kinase domain ofhuman RSK1. Acta Crystallographica Section D: Biological Crystallography 2012, 68 (6), 680-685.

3.   Liu, C.; Zhao, M.; Jiang, L.; Cheng, P.; Park,J.; Sawaya, M. R.; Pensalfini, A.; Gou, D.; Berk, A. J.; Glabe, C. G.; Nowick,J.*; Eisenberg, D.*, Out-of-register β-sheets suggest a pathway to toxicamyloid aggregates. Proceedings of the National Academy of Sciences 2012, 109(51), 20913.

4.   Laganowsky, A.; Liu, C.; Sawaya, M. R.; Whitelegge,J. P.; Park, J.; Zhao, M.; Pensalfini, A.; Soriaga, A. B.; Landau, M.; Teng, P.K.; Cascio, D.; Glabe, C.; Eisenberg, D.*, Atomic View of a Toxic Amyloid SmallOligomer. Science 2012, 335 (6073), 1228.

5.   Cheng, P.-N.; Liu, C.; Zhao, M.; Eisenberg,D.*; Nowick, J. S.*, Amyloid β-sheet mimics thatantagonize protein aggregation and reduce amyloid toxicity. Nature chemistry 2012, 4(11), 927-933.

2011

1.   Liu, C.; Sawaya, M. R.; Eisenberg, D.*, β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils withdisulfide linkages. Nature structural & molecular biology 2011, 18(1), 49.

2.   Zheng, J.; Liu, C.; Sawaya, M. R.; Vadla, B.;Khan, S.; Woods, R. J.; Eisenberg, D.; Goux, W. J.; Nowick, J. S.*, Macrocyclicβ-sheet peptides that inhibit the aggregation of a tau-protein-derivedhexapeptide. Journal of the American Chemical Society 2011, 133(9), 3144-3157.

3.   Liu, C.; Sawaya, M. R.; Cheng, P.; Zheng, J.;Nowick, J. S.; Eisenberg, D.*, Characteristics of amyloid-related oligomersrevealed by crystal structures of macrocyclic β-sheet mimics. Journalof the American Chemical Society 2011, 133 (17), 6736-6744.