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ZANG Jianye, Professor, Hundred Talents Program Structure and Function of Biomacromolecules
Name:  Jianye Zang (臧建业)
Born:   March 27, 1976, Jiangsu, P. R. China
Address: School of life science, University of Science and Technology of China, Hefei, Anhui 230027, P. R. China
Tel: 86-551-63603433
Fax: 86-551-63603433
E-mail: zangjy@ustc.edu.cn
 
EDUCATION AND RESEARCH EXPERIENCE
 1994-1998 Bachelor, University of Science and Technology of China, China
 1998-2003 Ph. D, University of Science and Technology of China, China
 2003-2007 Post-doctoral fellow, National Jewish Medical and Research Center, UCHSC, USA
 2007- Present Professor, University of Science and Technology of China, China
 
RESEARCH INTERESTS
1) Structural basis of epigenetic inheritance
2) Structural basis of immune escape of pathogens
 
CURRENT RESEARCH PROJECTS
1) Structural basis for protein modification, Ministry of Science & Technology of China
2) Study the structural and functional roles of RNA degradosome of Staphylococcus aureus, National Natural Science Foundation of China
3) Structural biological research of histone demethylases toward H3K36, National Natural Science Foundation of China
 
REPRESENTATIVE PUBLICATIONS
1) Wang, H., Zhou, X., Wu, M., Wang, C., Zhang, X., Tao, Y., Chen, N. and Zang, J. (2013) Structure of the JmjC-domain-containing protein JMJD5. Acta Crystallogr D Biol Crystallogr, 69, 1911-1920.
2) Tao, Y., Wu, M., Zhou, X., Yin, W., Hu, B., de Crombrugghe, B., Sinha, K.M. and Zang, J. (2013) Structural Insights into Histone Demethylase NO66 in Interaction with Osteoblast-specific Transcription Factor Osterix and Gene Repression. J Biol Chem, 288, 16430-16437.
3) Wu, M., Tao, Y., Liu, X. and Zang, J. (2013) Structural Basis for Phosphorylated Autoinducer-2 Modulation of the Oligomerization State of the Global Transcription Regulator LsrR from Escherichia coli. J Biol Chem, 288, 15878-15887.
4) Zhang, X., Chen, J., Wu, M., Wu, H., Arokiaraj, A.W., Wang, C., Zhang, W., Tao, Y., Huen, M.S. and Zang, J. (2013) Structural basis for role of ring finger protein RNF168 RING domain. Cell Cycle, 12, 312-321.
5) Ruan, J., Xu, C., Bian, C., Lam, R., Wang, J.P., Kania, J., Min, J. and Zang, J. (2012) Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1. FEBS Lett, 586, 314-318.
6) Li, J., Wang, C., Wu, Y., Wu, M., Wang, L., Wang, Y. and Zang, J. (2012) Crystal structure of Sa239 reveals the structural basis for the activation of ribokinase by monovalent cations. J Struct Biol, 177, 578-582.
7) Bian, C., Xu, C., Ruan, J., Lee, K. K., Burke, T. L., Tempel, W., Barsyte, D., Li, J., Wu, M., Zhou, B. O., Fleharty, B. E., Paulson, A., Allali-Hassani, A., Zhou, J. Q., Mer, G., Grant, P. A., Workman, J. L.*, Zang, J.* & Min, J.* (2011). Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. EMBO J 30, 2829-42. (*Co-corresponding author)
8) Wang, L., Wu, M. & Zang, J. (2011). Crystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus. J Struct Biol 174, 413-9.
9) Hong, X.*, Zang, J.*, White, J.*, Wang, C., Pan, C. H., Zhao, R., Murphy, R. C., Dai, S., Henson, P., Kappler, J. W., Hagman, J. & Zhang, G. (2010). Interaction of JMJD6 with single-stranded RNA. Proc Natl Acad Sci USA 107, 14568-72. (*Co-first author)
10) Liu, Y., Huang, H., Zhou, B. O., Wang, S. S., Hu, Y., Li, X., Liu, J., Zang, J., Niu, L., Wu, J., Zhou, J. Q., Teng, M. & Shi, Y. (2010). Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing. J Biol Chem 285, 4251-62.
11) Lai, C., Wu, M., Li, P., Shi, C., Tian, C. & Zang, J. (2010). Solution NMR characterization of Sgf73(1-104) indicates that Zn ion is required to stabilize zinc finger motif. Biochem Biophys Res Commun 397, 436-40.
12) Wang, J., Zhang, W., Song, W., Wang, Y., Yu, Z., Li, J., Wu, M., Wang, L., Zang, J. & Lin, Q. (2010). A biosynthetic route to photoclick chemistry on proteins. J Am Chem Soc 132, 14812-8.
13) Zhu, Z., Gao, Y., Yu, Y., Zhang, X., Zang, J., Teng, M. & Niu, L. (2009). Structural basis of the autolysis of AaHIV suggests a novel target recognizing model for ADAM/reprolysin family proteins. Biochem Biophys Res Commun 386, 159-64.
14) Chen, Z., Zang, J., Kappler, J., Hong, X., Crawford, F., Wang, Q., Lan, F., Jiang, C., Whetstine, J., Dai, S., Hansen, K., Shi, Y. & Zhang, G. (2007). Structural basis of the recognition of a methylated histone tail by JMJD2A. Proc Natl Acad Sci USA 104, 10818-23.
15) Chen, Z.*, Zang, J.*, Whetstine, J., Hong, X., Davrazou, F., Kutateladze, T. G., Simpson, M., Mao, Q., Pan, C. H., Dai, S., Hagman, J., Hansen, K., Shi, Y. & Zhang, G. (2006). Structural insights into histone demethylation by JMJD2 family members. Cell 125, 691-702. (*Co-first author)
16) Wang, D., Guo, M., Liang, Z., Fan, J., Zhu, Z., Zang, J., Li, X., Teng, M., Niu, L., Dong, Y. & Liu, P. (2005). Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites. J Biol Chem 280, 22962-7.

 


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