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 Zhijie Liu, Professor
 刘志杰研究员

Biography & Introduction

1995:Ph.D. Protein Crystallography, Institute of Biophysics, Chinese Academy of Sciences

1995:Postdoc,Department of Crystallography, University of Pittsburgh

1997:Postdoc,Department of Biochemistry & Molecular Biology,University of Georgia

2002:Assistant Research Scientist,Department of Biochemistry & Molecular Biology   University of Georgia

2005:Associate Research Scientist, Southeast Collaboratory for Structural Genomics (SECSG), Department of Biochemistry & Molecular Biology, University of Georgia

2005:Professor,Institute of Biophysics, Chinese Academy of Sciences

The major research interests are focused on the following areas: (1) Structural and functional analysis of proteins and multi-protein complexes in innate immune signaling pathway; (2) Structural proteomics of human liver disease related proteins and structure based drug design; (3) Development of new methods and new technologies in protein X-ray crystallography.

Visit my Group Page Here >>> http://zjliulab.ibp.ac.cn/

 

Selected Publications (Since group established in 2005)

1.  Niu, F.$, Shaw, N. $, Wang, Y. $, Jiao, L. $, Ding, W., Li, X., Zhu, P., Upur, H., OuYang, S*,Cheng, G*, and Liu, Z. J*, (2013) Structure of the Leanyer Orthobunyavirus Nucleoprotein-RNA complex reveals novel architecture for RNA encapsidation, PNAS, doi: 10.1073/pnas.1300035110. ($: equal contribution)

2.  Ru, H. $, Ni, X. $, Zhao, L. $, Crowley, C., Ding, W., Hung, L., Shaw, N., Cheng, G*. and Liu, Z. J*, (2013) Structural basis for termination of AIM2-mediated signaling by p202. Cell Research, doi: 10.1038/cr.2013.52. ($: equal contribution)

3.  Jiao, L. $, OuYang, S.$, N. $, Liang, M. $, Niu, F. $, Shaw, N., Wu, W., Ding, W., Jin, C., Peng, Y., Zhu, Y., Zhang, F., Wang, T., Li, C., Zuo, X., Luan, C.*, Li., D.*, and Liu, Z. J*, (2013) Structure of Severe Fever with Thrombocytopenia Syndrome Virus Nucleocapsid protein in Complex with Suramin Reveals Therapeutic Potentials. J. VI, doi: 10.1128/JVI.00672-13. ($: equal contribution)

4.  Won, E, Xie, Y, Takemoto, C, Chen, L, Liu, Z. J, Wang, B. C, Lee, D, Woo, E, Park, S, Shirouzu, M, Yokoyama, S, Kim, S and Chi, S, (2013) High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26, Acta Cryst D, in press.

5.  Eremeeva, E.$, Natashin, P.$, Song, L., Zhou, Y., Berkel, W., Liu, Z. J*, Vysotski, E*.,  (2013) Oxygen Activation of Apo-obelin–Coelenterazine Complex, Chem BioChem, DOI: 10.1002/cbic.201300002. ($: equal contribution)

6.  OuYang, S, Song, X, Wang, Y, Ru, H., Shaw, N., Jiang, Y., Niu, F., Zhu, Y., Qiu, W., Parvatiyar, K., Li, Y., Zhang, R., Cheng, G*., and Liu, Z. J*, (2012) Structural Analysis of the STING Adaptor Protein Reveals a Hydrophobic Dimer Interface and Mode of Cyclic di-GMP Binding, Immunity, 36(6): 1073-1086.

7.  Parvatiyar, K., Zhang, Z., Teles, R. M., Ouyang, S., Jiang, Y., Iyer, S. S., Zaver, S. A., Schenk, M., Zeng, S., Zhong, W., Liu, Z. J., Modlin, R. L., Liu, Y. J*., and Cheng, G*. (2012) The helicase DDX41 recognizes the bacterial secondary messengers cyclic di-GMP and cyclic di-AMP to activate a type I interferon immune response, Nat Immunol 13, 1155-1161.

8.  Shaw, N., OuYang, S,and Liu, Z. J*, (2012) Binding of bacterial secondary messenger molecule c di-GMP is a STING operation, Protein & Cell, Epub date 2012/12/25, DOI 10.1007/s13238-012-2071-0.

9.  Ru, H., Zhao, L., Ding, W., Jiao, L., Shaw, N., Liang, W., Zhang, L., Hung, L., Matsugaki, N., Wakatsuki, S. and Liu, Z. J*,  (2012) The S-SAD phasing study of DR6 and its solution conformation revealed by SAXS. Acta Cryst, D68, 521–530.

10. Zhan, Z., OuYang, S., Liang, W., Zhang, Z., Liu, Z. J* and Huang, L.*, (2012) Structural and functional characterization of the C-terminal catalytic domain of the SSV1 integrase. Acta Cryst D68, 659–670.

11. Hua, T., Wu, D., Ding, W., Wang, J., Neil, N*., and Liu, Z. J*, (2012) Studies on human 2, 4 dienoyl CoA reductase (DCR) sheds new light on peroxisomal β-oxidation of unsaturated fatty acids, J Biol Chem, 287(34):28956-65.

12. OuYang, S, Gong, B., Li, J., Zhao, L., Li, C., Wang, S., Pan, M., Liang, W., Shaw, N., Wu, W., Zhang, F., Sun, L., Zheng, J., Zhao, G., Wang, Y.*, Liu, Z. J.*, Liang, M.*. (2012) Structural insights into a human anti-IFN antibody exerting therapeutic potential for systemic lupus erythematosus. J. Mole Med, 90(7):837-846.

13. Yoshikawa, S., Kukimoto-Niino, M., Parker, L., Handa, N., Terada, T., Fujimoto, T., Terazawa, Y., Wakiyama, M., Sato, M., Sano, S., Kobayashi, T., Tanaka, T., Chen, L., Liu, Z. J., Wang, B. C., Shirouzu, M., Kawa, S., Semba, K., Yamamoto, T., Yokoyama, S. (2012) Structural basis for the altered drug sensitivities of non-small cell lung cancer-associated mutants of human epidermal growth factor receptor, Oncogene, 10.1038/onc.2012.21.

14. Titushin, M., Feng, Y., Lee, J., Vysotski, E. & Liu, Z. J*. (2011) Protein-protein complexation in bioluminescence. Protein & Cell, 2(12): 957-972. (Cover)

15. Liu, Z. J*, Chen, L., Wu, D., Ding, W., Zhang H., Zhou, W., Fu, Z. & Wang, BC*, (2011) A multi-dataset data-collection strategy produces better diffraction data. Acta Cryst A67, 544-549.

16. Liang, W., SongYing, O., Shaw, N., Joachimiak, A., Zhang, RG, & Liu, Z. J*. (2011) Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE. Faseb J., 25(2): 497-504.

17. Titushin, M., Feng, Y., Stepanyuk, G., Li, Y., Markova, S, Golz, S., Wang, BC, Lee, J., Wang, J., Vysotski, E. & Liu, Z. J*. (2010) NMR derived topology of a GFP-photoprotein energy transfer complex. J Biol Chem, 285(52): 40891–40900.

18. Zhou, Y., Shaw, N., Li, Y., Zhao, Y, Zhang, RG, & Liu, Z. J*. (2010) Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules. Faseb J., 24(12): 4668-4677.

19. Su, J., Li, Y., Shaw, N., Zhou, WH, Zhang, M., Xu, H., Wang, BC, & Liu, Z. J*. (2010) Crystal structure of a novel non-Pfam protein PF2046 solved using low resolution B-factor sharpening and multi-crystal averaging methods. Protein & Cell, 1(5): 453–458.

20. Wu, D., Li, Y., Song, GJ, Zhang, R., Joachimiak, A., Shaw, N., & Liu, Z. J*. (2009) Structural basis for the inhibition of human MTHFS by N10-substituted folate analogues. Cancer Research, 69(18), 7294-301. (Cover)

21. Wu, D., Li, Y., Song, GJ, Shaw, N., & Liu, Z. J*. (2009) Crystal structure of human esterase D: a potential genetic marker of retinoblastoma. Faseb J., 23(5), 1441-1446.

22. Song, G., Li, Y., Cheng, C., Zhao, Y., Gao, A., Zhang, R., Joachimiak, A., Shaw, N., & Liu, Z. J*. (2009) Structural insight into acute intermittent porphyria. Faseb J., 23(2), 396-404.

23. Natalia Moiseeva, Robert Bau, Stephen D. Swenson, Francis S. Markland, Jun-Yong Choe, Liu, Z. J and Marc Allaire, (2008) Structure of acostatin, a dimeric disintegrin from Southern copperhead (Agkistrodon contortrix contortrix), at 1.7 Å, Acta Cryst D64, 466–470.

24. Shaw, N., Zhao, M., Cheng, C., Xu, H., Saarikettu, J., Li, Y., Da, Y., Yao, Z., Silvennoinen, O., Yang, J.*, Liu, Z. J*., Wang, B. C. & Rao, Z. (2007) The multifunctional human p100 protein 'hooks' methylated ligands. Nat Struct Mol Biol, 14(8), 779-84.

25. Shaw, N., Cheng, C., and Liu, Z. J*, (2007) Procedure for reductive methylation of protein to improve crystallizability. Nature Protocols ,DOI: 10.1038/nprot.2007.287

26. Handa, N., Kishishita, S., Morita, S., Akasaka, R., Jin, Z., Chrzas, J., Chen, L., Liu, Z. J., Wang, B. C., Sugano, S., Tanaka, A., Terada, T., Shirouzu, M. & Yokoyama, S. (2007) Structure of the human tim44 c-terminal domain in complex with pentaethylene glycol: Ligand-bound form. Acta Cryst D63(12), 1225-1234.

27. Kondo, N., Nakagawa, N., Ebihara, A., Chen, L., Liu, Z. J., Wang, B. C., Yokoyama, S., Kuramitsu, S. Masui, R. (2007). Structure of dNTP-inducible dNTP triphosphohydrolase: insight into broad specificity for dNTPs and triphosphohydrolase-type hydrolysis. Acta Cryst D63, 230-9.

28. Liu, Z.J., Stepanyuk, G.A., Vysotski, E.S., Lee, J., Markova, S.V., Malikova, N.P., and Wang, B.C. (2006). Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state. Proc Natl Acad Sci 103, 2570-2575.

Contact: 

E-mail  zjliu(AT)ibp.ac.cn(请将(AT)替换为@,防止垃圾邮件)

Tel

 010-64857988

Fax

 010-64888426
Postalcode  100101