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TENG Maikun, Professor Structure and Function of Biomacromolecules
Name:  Maikun Teng (滕脉坤)
Born:   1956.01
Address: School of Life Science, University of Science and Technology of China, Hefei, Anhui 230027, P. R. China
Tel: 86-551-63606314
Fax: 86-551-63606314
E-mail: mkteng@ustc.edu.cn

1). F. Zeng, W. Zhang, N. Xue, M. Teng, X. Li, B. Shen, Crystal structure of phospholipase PA2-Vb, a protease-activated receptor agonist from the Trimeresurus stejnegeri snake venom, FEBS LETTERS 588(24): 4604-4612, (2014).
2). Z. Liu, P. Chen a, X. Wang, G. Cai, L. Niu, M. Teng, & X. Li, Crystal structure of DnaT84-153-dT10 ssDNA complex reveals a novel single-stranded DNA binding mode, Nucleic Acids Res. 42, 9470-9483, (2014).
3).  Z. Shao, W. Yan, J. Peng, X. Zuo, Y. Zou, F. Li, D. Gong, R. Ma, J. Wu, Y. Shi, Z. Zhang, M. Teng, X. Li, Q. Gong, Crystal structure of tRNA m(1)G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate, NUCLEIC ACIDS RESEARCH, 42, 509-525,(2014).
4). H. Liu, H. Wang, M. Teng, X. Li, The multiple nucleotide-divalent cation binding modes of Saccharomyces cerevisiae CK2 alpha indicate a possible co-substrate hydrolysis product (ADP/GDP) release pathway, Acta Cryst. D70, 501-513, (2014).
5). F. Zeng, Z. Zou, L. Niu, X. Li, & M. Teng, AhV_aPA-induced vasoconstriction involves the IP3Rs-mediated Ca2+ releasing, Toxicon, 70, 107-113, (2013).
6). W. Zhang, F. Zeng, Y. Liu, Y. Zhao, H. Lv, L. Niu, M. Teng & X. Li, Crystal Structures and RNA-Binding Properties of the RRMs of hnRNP-L: Insights into Its Roles in Alternative-splicing Regulation, J. Biol. Chem., 288, 22636-49, (2013).
7). Y. Zhu, J. Dai, T. Zhang, P. Fang, H. Wang, Y. Jiang, X. Yu, T. Xia, L. Niu, Y. Guo & M. Teng, Structural insights into the neutralization mechanism of mAb 6C2 against ricin, J. Biol. Chem., 288, 25165-72, (2013).
8). H. Liu, Y. Gao, M. Zhang, X. Qiu, A. J. L. Cooper, L. Niu and M. Teng, Structures of enzyme–intermediate complexes of yeast Nit2: insights into its catalytic mechanism and different substrate specificity compared with mammalian Nit2, Acta Cryst. D69, 1470-81, (2013).
9). Y. Tao, C. Jin, X. Li, S. Qi, L. Chu, L. Niu, X. Yao & M. Teng, The structure of the FANCM-MHF complex reveals physical features for functional assembly, Nature Communications, 3, 782, Apr 17; doi:10.1038/ncomms1779, (2012).
10). J. Wang, M. Gossing, P. Fang, J. Zimmermann, X. Li, G. F. von Mollard, L. Niu, and M. Teng, Epsin N-terminal homology domains bind on opposite sides of two SNAREs, Proc Natl Acad Sci USA, 108 (30):12277-82; (2011).
11). P. Fang, X. Li, J. Wang, L. Niu and M. Teng, Structural basis for the specificity of GAE domain of yGGA2 for its accessory proteins Ent3 and Ent5,Biochemistry, 49(36), 7949-55, (2010).
12). Y. Liu, Y. Hu, X. Li, L. Niu, M. Teng, Crystal structure of human nascent polypeptide-associated complex domain reveals a nucleic acid-binding region on the NACA subunit,Biochemistry, 49(13): 2890-6, (2010).
13). Y. Liu, H. Huang, B. Zhou, S. Wang, Y. Hu, X. Li, J. Liu, J. Zang, L. Niu, J. Wu, J. Zhou, M. Teng and Y. Shi, Structural analysis of Rtt106p reveals a DNA-binding role required for heterochromatin silencing, J. Biol. Chem., 285,4251-4262, (2009).
14). J. Wang, B. Shen, M. Guo, X. Lou, Y. Duan, X. Cheng, M. Teng, L. Niu, Q. Liu, Q. Huang, Q. Hao, (2005), The Blocking Effect and Crystal Structure of Natrin Toxin, a CRISP Protein from Naja atra Venom that Targets BKCa Channel; Biochemistry-US, 44,10145-10152.
15). M. Guo, M. Teng, L. Niu, Q. Liu, Q. Huang, and Q. Hao, (2005), Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold, J. Biol. Chem., 280, 12405 – 12412.
16). Y. Ghendler, M. Teng, J. Liu, T. Witte, J. Liu, K. Kim, P. Kern, H. Chang, J. Wang and E. Reinherz, (1998), Differential thymic selection outcomes stimulated by focal structural alteration in peptide/MHC ligands, Proc. Natl. Acad. Sci. U.S.A., 95, 10061-10066.
17). M. Teng, et al, (1998), Crystal Structure of N15 TCR in Complex with its Peptide/MHC(pMHC) Ligand: Identification of a common docking topology with substantial variation among different TCR-pMHC complexes, Current Biology, 8, 409-412.

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