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1. Versatile Structures of a-Synuclein. (review)

Wang C.C., Zhao C.Y., Li D., Tian Z.Q., Lai Y., Diao J.J.*, Liu C.*

Frontiers in Molecular Neuroscience, 2016, 9, 48. (* corresponding author)


2.Precise and reversible protein microtubule-like structure with helicity driven by dual supramolecular interactions.

Yang G., Zhang X., Kochovshi Z., Zhang Y., Dai B., Sakai F., Jiang L., Lu Y., Ballauff M., Li X., Liu C.*, Chen G.*, Jiang M. 

J. Am. Chem. Soc., 2016, 138, 1932-1937. (* corresponding author)


3.Tunable assembly of amyloid-forming prptides into nanosheets as a retrovirus carrier.

Dai B., Li D., Xi W.H., Luo F., Zhang X., Zou M., Cao M., Hu J., Wang W.Y., Wei G.H.*, Zhang Y.*, Liu C.*

Proc. Natl. Acad. Sci. USA., 2015, 112, 2996-3001. (* corresponding author)


4. Structure-based design of functional amyloid materials.

Li D., Jones E.M., Sawaya M.R., Furukawa H., Luo F., Ivanova M., Sievers S.A., Wang W.Y., Yaghi O.M., Liu C., Eisenberg D.S.

J. Am. Chem. Soc., 2014, 136, 18044-188051.


5. Antiparalle triple-strand architecture for prefibrillar Abeta42 oligomers.

Gu L., Liu C., Stroud J.C., Ngo S., Jiang L., Guo Z.

J. Biol. Chem., 2014, 289, 27300-27313.


6.The structured core domain of aB-crystallin can prevent amyloid fibrillation and associated toxicity.

 Hochberg G.K.A., Ecroyd H., Liu C., Cox D., Cascio D., Sawaya M.R., et al.  

Proc. Natl. Acad. Sci. U.S.A., 2014, 111, 1562-1570.


7. Designed amyloid fibers as materials for selective carbon dioxide capture.

Li D., Furukawa H., Deng H, Liu C., Yaghi O.M., Eisenberg D.S.  

Proc. Natl. Acad. Sci. U.S.A., 2014, 111, 191-96.


8. Structure-baseddiscovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta.

Jiang L.¶, Liu C., Leibly D., Landau M., Zhao M.L., Hughes M., et al 

Elife, 2013, 00857. (¶ Authors contributed equally)


9. Structure insights into Aβ42 oligomers using site-directed spin labeling.

Gu L., Liu C., Guo Z.  

J. Biol. Chem., 2013, 288, 18673-18683.


10. Out-of-register β-sheets suggest a pathway to toxicamyloid aggregations. 

Liu C., Zhao M.L.¶, Jiang L.¶, Cheng P.N., Park J.Y., Sawaya M., et al

Proc. Nat. Acad. Sci. U.S.A., 2012, 109, 0913-0918. (¶ Authors contributed equally)


11. Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity. 

Cheng P.N.¶, Liu C., Zhao M.L., Eisenberg D. and Nowick J.  

Nat. Chem., 2012, 4, 927-933. (¶ Authors contributed equally)


12. Structural basis forthe autoinhibition of the C-terminal kinase domain of human RSK1.

Li D., Fu T.M., Nan J., Liu C., Li L.F., and Su X.D.  

Acta Crystallogr. D, 2012, 68, 680-685.


13.Toxic fibrillar oligomers of amyloid-β have cross-β structure. 

Stroud J.C.¶, Liu C., Teng P.K. and Eisenberg D. 

Proc. Nat. Acad. Sci. U.S.A., 2012, 109, 7717-7722. (¶ Authors contributed equally)


14. Atomic view of a toxic amyloid small oligomer.

Laganowsky A., Liu C., Sawaya M.R., Whitelegge J.P., Park J., Zhao M., et al 

Science, 2012, 335, 1228-1231.


15. Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics.

Liu C., Sawaya M.R.¶, Cheng P.N., Zheng J., Nowick J.S. and Eisenberg D.  

J. Am. Chem. Soc., 2011, 133, 6736-6744. (¶ Authors contributed equally)


16. Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.

Zheng J., Liu C., Sawaya M.R., Vadla B., Khan S., Woods R.J., et al 

J. Am. Chem. Soc., 2011, 133, 3144-3157.


17. β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.

Liu C., Sawaya M.R. and Eisenberg D.  

Nat. Struct. Mol. Biol., 2011, 18, 49-55.


18. Structure and novel functional mechanism of Drosophila SNF in sex-lethal splicing. 

Hu J., Cui G., Li C., Liu C., Shang E., Lai L., et al. 

PloS one, 2009, 4, e6890.


19. Crystal structure of B. subtilis YjcG characterizing the YjcG-like group of 2H phosphoesterase superfamily. 

Li D.¶, Liu C., Liang Y.H.,  Li L.F. and Su X.D. 

Proteins: Structure, Function, and Bioinformatics, 2008, 72, 1071-1076. (¶ Authors contributed equally)


20. Ring-opening mechanism revealed by crystal structures of NagB and its ES intermediate complex. 

Liu C., Li D.¶, Liang Y.H., Li L.F. and Su X.D. 

J. Mol. Biol., 2008, 379, 73-81. (¶ Authors contributed equally)

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