|Dr. Bai obtained her B.S. degree from Peking University in 2003. She conducted graduate research at Columbia University and obtained her Ph.D. degree in 2010. From 2010 to 2015, she received postdoctoral training at University of California, Berkeley. In January 2016, Dr. Bai joined ShanghaiTech University as a tenure-track assistant professor, PI in the School of Life Science and Technology.|
|RNA molecules not only serve as carriers of genetic information but also play key roles in the control of various cellular processes. These regulatory functions oftentimes rely on specific RNA structures, interactions with RNA-binding proteins (RBPs), or both. To date, a thorough understanding of the rules in RNA structure formation and how that affects RBP recognition remains a grand challenge. Using a combination of molecular, systems and structural biology methods, research in Bai lab will focus on understanding how RNA structures facilitate partner interactions and biological functions. This will not only bring mechanistic insights into key biological processes but also provide new therapeutic targets for RNA-related diseases, such a cancer and neurodegenerative diseases.|
|1. Y. Bai, A. Tambe, K. Zhou & J.A. Doudna. (2014) RNA-guided assembly of Rev-RRE nuclear export complexes. eLife, 3, e03656. |
2. Y. Bai, K. Zhou & J.A. Doudna. (2013) Hepatitis C virus 3’UTR regulates viral translation through direct interactions with the host translation machinery. Nucleic Acids Res., 41, 7861- 7874.
3. K.E. Berry, S. Waghray, S.A. Mortimer, Y. Bai & J.A. Doudna. (2011) Crystal structure of the HCV IRES central domain reveals strategy for start-codon positioning. Structure, 19, 1456- 1466.
4. C. Sun, A. Todorovic, J. Querol-Audi, Y. Bai, N. Villa, M. Snyder, J. Ashchyan, C.S. Lewis, A. Hartland, S. Gradia, et al. (2011). Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3). Proc Natl Acad Sci U S A 108, 20473-20478.
5. Y. Bai, S. Srivastava, J.H. Chang, J.L. Manley & L. Tong. (2011) Structural basis for dimerization and activity of human PAPD1, a noncanonical poly(A) polymerase. Mol. Cell, 41, 311-320.
6. C.R. Mandel, Y. Bai & L. Tong. (2008). Protein factors in pre-mRNA 3’-end processing. Cell. Mol. Life Sci. 65, 1099-1122.
7. Y. Bai, T.C. Auperin, C.-Y. Chou, G.-G. Chang, J.L. Manley & L. Tong. (2007). Crystal structure of murine CstF-77: Dimeric association and implications for polyadenylation of mRNA precursors. Mol. Cell, 25, 863-875.
8. Y. Bai, T.C. Auperin & L. Tong. (2007). The use of in situ proteolysis in the crystallization of murine CstF-77. Acta Cryst. F63, 135-138.
9. M.J. Rudolph, G.A. Amodeo, Y. Bai & L. Tong. (2005). Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1. Biochem. Biophys. Res. Commun. 337, 1224-1228.