Research > Team II:Structure-Based Drug Design Discovery



Name Mark Bartlam
Research Area

The study of key proteins involved in protein and mRNA degradation and quality control; 
The study of key proteins involved in cell cycle regulation; 
The study of essential proteins for the survival and virulence of pathogenic bacteria.

Tel 0086-22-23502351
E-mail bartlam@nankai.edu.cn
Brief
Introduction

    Mark Bartlam obtained his BSc degree in Physics from Imperial College London, UK in 1995, and his PhD degree from Oxford University, UK in 1999. He came to China in 2000 and worked in Tsinghua University and the Institute of Biophysics, Chinese Academy of Sciences, as a foreign expert. He joined Nankai University in 2007 as a specially appointed professor. He is currently Professor of Biochemistry in the College of Life Sciences, and group leader in the State Key Laboratory of Medicinal Chemical Biology in Nankai University. He was awarded Changjiang Scholar by the Ministry of Education, China in 2012. He received the Tianjin Haihe Friendship Award in 2010 and the China National Friendship Award in 2011.
Resent Publications (in 5 years)
1.      Yang W, Chen WY, Wang H, Ho JW, Huang JD, Woo PC, Lau SK, Yuen KY, Zhang Q, Zhou W, Bartlam M*, Watt RM*, Rao Z. 2011. Structural and functional insight into the mechanism of an alkaline exonuclease from Laribacter hongkongensis. Nucleic Acids Res. 39(22):9803-9819.
2.      Yu, J., X. Li, Y. Wang, B. Li, H. Li, Y. Li, W. Zhou, C. Zhang, Y. Wang, Z. Rao, M. Bartlam*, and Y. Cao*. 2011. PDlim2 selectively interacts with the PDZ binding motif of highly pathogenic avian H5N1 influenza A virus NS1. PLoS ONE 6(5):e19511
3.      Wang, H, M. Morita, X. Yang, T. Suzuki, W. Yang, J. Wang, K. Ito, Q. Wang, C. Zhao, M. Bartlam*, T. Yamamoto*, and Z. Rao. 2010. Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity. EMBO J. 29(15):2566-76.
4.      Yang W, Bell SG, Wang H, Zhou W, Bartlam M*, Wong LL, Rao Z. 2010.The structure of CYP101D2 unveils a potential path for substrate entry into the active site. Biochem J. 433(1):85-93.
5.      Yuan, P., M. Bartlam, Z. Lou, S. Chen, J. Zhou, X. He, Z. Lv, R. Ge, X. Li, T. Deng, E. Fodor, Z. Rao, and Y. Liu, 2009. Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458: 909-13.