JASON PHAN, Ph.D.
Research Assistant Professor of Biochemistry
Office: 804-A RRB
Jason Phan, Ph.D. is a Research Assistant Professor of Biochemistry and a structural biologist in the Fesik lab. His area of interest includes protein engineering, expression, purification and X-ray crystallography. Jason received his Ph.D. in Biochemistry at the University of South Carolina, Columbia in 2001 under the mentorship of Professor Lukasz Lebioda and postdoctoral training with Dr. David S. Waugh at the National Cancer Institute in Frederick, Maryland. At the end of 2005, he accepted a senior staff scientist position at the Moffitt Cancer Center in Tampa, Florida to build and operate a core facility for protein production and X-ray crystallography. Jason is a member of the American Crystallographic Association and a program member of the Vanderbilt-Ingram Cancer Center.
- Phan, J., J. A. Ross, P. H. Th’ng, C. G. Jakob and L. Lebioda. Protein crystal growth from biphasic systems. Curr. Top. Crystal Growth Res. (1997), 3, 223–228.
- Phan, J., E. Mahdavian, M. C. Nivens, W. Minor, S. H. Berger, H. T. Spencer, R. B. Dunlap and L. Lebioda. Catalytic Cysteine of Thymidylate Synthase Is Activated upon Substrate Binding. Biochemistry (2000), 39, 6969-6978.
- Fantz, C., D. Shaw, W. Jennings, A. Forsthoefel, M. Kitchens, J. Phan, W. Minor, L. Lebioda, F. G. Berger and H. T. Spencer. Drug-resistant Variants of Escherichia coli Thymidylate Synthase: Effects of Substitutions at Pro254. Mol. Pharmacol. (2000), 57, 359–366.
- Phan, J., D. J. Steadman, S. Koli, W. C. Ding, W. Minor, R. B. Dunlap, S. H. Berger and L. Lebioda. Structure of Human Thymidylate Synthase Suggests Advantages of Chemotherapy with Noncompetitive Inhibitors. J. Biol. Chem. (2001), 276, 14170–14177.
- Phan, J., S. Koli, W. Minor, R. B. Dunlap, S. H. Berger and L. Lebioda. Human Thymidylate Synthase Is in the Closed Conformation when Complexed with dUMP and Raltitrexed, an Antifolate Drug. Biochemistry (2001), 40, 1897–1902.
- Phan, J., A. Zdanov, A. G. Evdokimov, J. E. Tropea, H. K. III Peters, R. B. Kapust, M. Li, A. Wlodawer, and D. S. Waugh. Structural Basis for the Substrate Specificity of Tobacco Etch Virus Protease. J. Biol. Chem. (2002), 277, 50564–50572.
- Evdokimov, A.G., J. Phan, J. E. Tropea, K. M. Routzahn, H. K. III Peters, M. Pokross, and D. S. Waugh. Similar Modes of Polypeptide Recognition by Export Chaperones in Flagellar Biosynthesis and Type III Secretion. Nature Structural Biology (2003), 10, 789–793.
- Phan, J., K. Lee, S. Cherry, J. E. Tropea, T. R. Burke, Jr., and D. S. Waugh. High-Resolution Structure of the Yersinia Pestis Phosphatase YopH in Complex with a Phosphotyrosyl Mimetic-Containing Hexapeptide. Biochemistry, (2003), 42, 13113–13121.
- Lee, K., Y. Gao, Z.-J. Yao, J. Phan, L. Wu, J. Liang, D. S. Waugh, Z.-Y. Zhang, and T. R. Burke, Jr. Tripeptide Inhibitors of Yersinia Protein-Tyrosine Phosphatase as Potential Therapeutic Leads for the Treatment of Plague. Bioorg. Med. Chem. Lett. (2003), 13, 2577–2581.
- Phan, J., J. E. Tropea, and D. S. Waugh. Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2. Acta Cryst, (2004), 60, 1591–1999.
- Phan, J., Z.-D. Shi, T. R. Burke Jr., and D. S. Waugh. Crystal Structures of a High-Affinity Macrocyclic Peptide Mimetic in Complex with the Grb2 SH2 Domain. J. Mol. Biol., (2005), 353, 104 –115.
- Phan, J., B. Austin, and D. S. Waugh. Crystal structure of the Yersinia pestis type III secretion protein YscE. Protein Sci., (2005), 14, 2759– 2763.
- Tropea, J.E., Phan, J., and Waugh, D. S. Overproduction, purification, and biochemical characterization of the dual specificity H1 protein phosphatase encoded by variola major virus. Protein Expr. Purif., (2006) 50, 31–36.
- Phan, J., J. E. Tropea, and D. S. Waugh. Structure-Assisted Discovery of Variola major H1 Phosphatase Inhibitors. Acta Cryst. (2007). D63, 698-704.
- Phan, J., Li Z, Kasprzak A, Li B, Sebti S, Guida W, Schönbrunn E, Chen J. Structure-based design of high affinity peptides inhibiting the interaction of p53 with MDM2 and MDMX. J Biol Chem. (2010) 285, 2174-83.