Xiaoqiang Wang

Xiaoqiang Wang, PhD

Professor of Biochemistry, College of Pharmacy

Nankai University, Tianjin, China

Xiaoqiang Wang received his Bachelor’s and Master’s degrees in physical chemistry from Wuhan University in 1987 and 1990, respectively. He obtained his Ph.D. in molecular biology from Institute of Biophysics, Chinese Academy of Sciences, Beijing, China in 1993, and worked as a Research Assistant/Associate Professor at the same institute from 1993 to 1995. He worked as a research associate at University of Manchester, UK (1995-1996), and in Oklahoma Medical Research Foundation (1996-1999). He was a research fellow in the National Institute of Environmental Health Sciences (NIEHS)/National Institutes of Health (NIH) from 1999 to 2002. He moved to the Noble Foundation, Oklahoma, USA in 2002 and worked as assistant and associate professor. He joined the State Key Laboratory of Medicinal Chemical Biology and College of Pharmacy at Nankai University in 2015. He is an editorial board member of “International Journal of Plant Biology & Research” and “Frontiers in Plant Metabolism and Chemodiversity”.

Dr. Xiaoqiang Wang’s research interests include natural product biosynthesis and protein structure and engineering, including biosynthetic enzymes, protein-RNA interaction, and protein-protein interaction. He first revealed molecular basis of glycosylation of natural products. His research is providing a basis for understanding the enzymatic mechanisms and biosynthetic processes, facilitating manipulation of enzymes and biosynthetic pathways toward bioactive natural products and drug discovery. He has published original research articles and review articles in the prestigious journals, e.g., Cell, Science, Molecular Cell,Plant Cell, Nature Structural Biology,Proc. Natl. Acad. Sci. USA, J. Mol. Biology, Pharmaceutical Research,and Current Drug Metabolism.

Selected Publications:

1. Xu, X., et al. (2016). De Novo Transcriptome Assembly and Annotation of the Leaves and Callus of Cyclocarya Paliurus (Bata1) Iljinskaja. PLoS One. 11(8): e0160279.

2. Zhao, Q., et al. (2013). Laccase is necessary and nonredundant with peroxidase for lignin polymerization during vascular development in Arabidopsis.Plant Cell. 25(10): p. 3976-87.

3. Wu, B., et al. (2012). Accurate prediction of glucuronidation of structurally diverse phenolics by human UGT1A9 using combined experimental and in silico approaches,Pharmaceutical Research.  29, 1544-1561.

4. Wu, B., et al. (2011). Regioselective sulfation and glucuronidation of phenolics: insights into the structural basis, Current Drug Metabolism. 12, 900-916.

5. Wang, X., Structure, function, and engineering of enzymes in isoflavonoid biosynthesis. Funct Integr Genomics, 2011. 11(1): p. 13-22.

6.Li, L., et al., Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp. Acta Crystallogr D Biol Crystallogr, 2010. 66(Pt 6): p. 725-32.

7.  Wang, X., Structure, mechanism and engineering of plant natural product glycosyltransferases. FEBS Lett, 2009. 583(20): p. 3303-9.

8. Modolo, L.V., et al., Single amino acid mutations of Medicago glycosyltransferase UGT85H2 enhance activity and impart reversibility. FEBS Lett,2009. 583(12): p. 2131-5.

9.Li, L., et al., Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase. Proc Natl Acad Sci U S A, 2008. 105(37): p. 13883-8.

10. Li, L., et al., Crystal structure of Medicago truncatula UGT85H2--insights into the structural basis of a multifunctional (iso)flavonoid glycosyltransferase. J Mol Biol, 2007. 370(5): p. 951-63.

11. Wang, X., et al., Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.). J Mol Biol, 2006. 358(5): p. 1341-52.

12. Shao, H., et al., Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula. Plant Cell, 2005. 17(11): p. 3141-54.

13.Wang, X., et al., Modular recognition of RNA by a human pumilio-homology domain. Cell, 2002. 110(4): p. 501-12.

14. Wang, X., P.D. Zamore, and T.M. Hall, Crystal structure of a Pumilio homology domain. Mol Cell, 2001. 7(4): p. 855-65.

15. Wang, X. and T.M. Tanaka Hall, Structural basis for recognition of AU-rich element RNA by the HuD protein. Nat Struct Biol, 2001. 8(2): p. 141-5.

16. Wang, X., et al., Crystal structure of the catalytic domain of human plasmin complexed with streptokinase. Science, 1998. 281(5383): p. 1662-5.

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