| 1. | Hang, T., Chen, W., Wu, M., Zhan, L., Wang, C., Jia, N., Zhang, X and Zang, J. (2019) Structural insights into the molecular mechanism underlying Sirt5-catalyzed desuccinylation of histone peptides, Biochem J 476, 211-223. |
| 2. | Fang, T., Chen, W., Sheng, Y., Yuan, S., Tang, Q., Li, G., Huang, G., Su, J., Zhang, X., Zang, J. and Liu, Y. (2019) Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein, Nature commun 10, 186. |
| 3. | Wang, C., Zhan, L., Wu, M., Ma, R., Yao, J., Xiong, Y., Pan, Y., Guan, S., Zhang, X. and Zang, J. (2018) Spindlin-1 recognizes methylations of K20 and R23 of histone H4 tail, FEBS lett 592, 4098-4110. |
| 4. | Chen, X., Wang, C., Zhang, X., Tian, T. and Zang, J. (2018) Crystal structures of the N-terminal domain of the Staphylococcus aureus DEAD-box RNA helicase CshA and its complex with AMP, Acta Crystallogr F Struct Biol Commun 74, 704-709. |
| 5. | Tian, T., Wang, C., Wu, M., Zhang, X. and Zang, J. (2018) Structural Insights into the Regulation of Staphylococcus aureus Phosphofructokinase by Tetramer-Dimer Conversion, Biochemistry 57, 4252-4262. |
| 6. | Tian, T., Li, X., Liu, Y., Wang, C., Liu, X., Bi, G., Zhang, X., Yao, X., Zhou, Z. H., and Zang, J. (2018) Molecular basis for CENP-N recognition of CENP-A nucleosome on the human kinetochore, Cell Res 28, 374-378. |
| 7. | Hang, T., Zhang, X., Wu, M., Wang, C., Ling, S., Xu, L., Gong, Q., Tian, C., Zhang, X. and Zang, J. (2018) Structural insights into a novel functional dimer of Staphylococcus aureus RNase HII, Biochem Biophys Res Commun 503, 1207-1213. |
| 8. | Zhou, X., Zheng, F., Wang, C., Wu, M., Zhang, X., Wang, Q., Yao, X., Fu, C., Zhang, X. and Zang, J. (2017) Phosphorylation of CENP-C by Aurora B facilitates kinetochore attachment error correction in mitosis, Proc Natl Acad Sci USA 114, E10667-E10676. |
| 9. | Zhang, Y., Wu, M., Hang, T., Wang, C., Yang, Y., Pan, W., Zang, J., Zhang, M., and Zhang, X. (2017) Staphylococcus aureus SdrE captures complement factor H's C-terminus via a novel 'close, dock, lock and latch' mechanism for complement evasion, Biochem J 474, 1619-1631. |
| 10. | Wang, X., Wang, C., Wu, M., Tian, T., Cheng, T., Zhang, X. and Zang, J. (2017) Enolase binds to RnpA in competition with PNPase in Staphylococcus aureus, FEBS lett. 591, 3523-3535. |
| 11. | Li, Y., Chen, X. B., Jia, N., Zhang, X. and Zang, J.(2017) Identification of Set11 from Staphylococcus aureus Mu50 strain as a ortholog of SSL7 via bioinformatic analysis and determination of its possible targets from human serum using CNBr-pull down assays, Biotechnol Lett 39, 1413-1423. |
| 12. | Chen, W., Wu, M., Hang, T., Wang, C., Zhang, X. and Zang, J. (2017) Structure insights into the molecular mechanism of the interaction between UHRF2 and PCNA, Biochem Biophys Res Commun 494, 575-580. |
| 13. | Wang C, Zhang Q, Hang T, Tao Y, Ma X, Wu M, Zhang X and Zang J. (2015). Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8. Acta Crystallogr D Biol Crystallogr 71:1955-64. |
| 14. | Song Y, Zhang F, Li X, Zang J. and Zhang X. (2015). Crystallographic studies of SarV, a global regulator from Staphylococcus aureus. Acta Crystallogr F Struct Biol Commun 71:1038-41. |
| 15. | Zhang W, Wang C, Song Y, Shao C, Zhang X. and Zang J. (2015). Structural insights into the mechanism of Escherichia coli YmdB: A 2'-O-acetyl-ADP-ribose deacetylase. J Struct Biol 192:478-86. |
| 16. | Wu Y, Wang C, Lin S, Wu M, Han L, Tian C, Zhang X and Zang J. (2015). Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate. Acta Crystallogr D Biol Crystallogr 71(Pt 12):2457-2470. |
| 17. | Shao, C., Wang, C. and Zang, J. (2014). Structural basis for the substrate selectivity of PvuRts1I, a 5-hydroxymethylcytosine DNA restriction endonuclease. Acta Crystallogr D Biol Crystallogr 70, 2477-86. |
| 18. | Wang, J., Liu, X., Dou, Z., Chen, L., Jiang, H., Fu, C., Fu, G., Liu, D., Zhang, J., Zhu, T., Fang, J., Zang, J., Cheng, J., Teng, M., Ding, X. and Yao, X. (2014). Mitotic regulator Mis18beta interacts with and specifies the centromeric assembly of molecular chaperone holliday junction recognition protein (HJURP). J Biol Chem 289, 8326-36 |
| 19. | 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. |
| 20. | Sun, D., Liu, Q., He, Y., Wang, C., Wu, F., Tian, C. and Zang, J. (2013). The putative propeptide of MycP1 in mycobacterial type VII secretion system does not inhibit protease activity but improves protein stability. Protein Cell 4, 921-31. |
| 21. | 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. |
| 22. | 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. |
| 23. | 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. |
| 24. | 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. |
| 25. | 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) |
| 26. | 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. |
| 27. | 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) |
| 28. | 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. |
| 29. | 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. |
| 30. | 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. |
| 31. | 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. |
| 32. | 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. |
| 33. | 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) |
| 34. | 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. |
