University of Maryland College Park
9600 Gudelsky Drive Room 4127C
Education and Training
I received a B.A. in Biochemistry from the University of Pennsylvania and a Ph.D. in Biochemistry from the University of California, Los Angeles (UCLA). I then conducted postdoctoral training at UCLA in the Department of Chemistry and Biochemistry and Harvard Medical School in the Department of Biological Chemistry and Molecular Pharmacology prior to joining the faculty at the University of Maryland in the Department of Biochemistry and Molecular Biology in 2004. In 2011, I became a Section Leader in Structural Biology in the Center for Biomolecular Therapeutics. I am a member of the Molecular and Structural Biology Program within the University of Maryland Marlene and Stewart Greenebaum Cancer Center Program in Oncology. As such, I collaborate with both basic and clinical research investigators to study the mechanisms of cancer development and metastasis and to identify candidate proteins that may serve as targets for therapeutic intervention.
As a Section Leader in Structural Biology at the Center for Biomolecular Therapeutics, I am responsible for using X-ray crystallographic techniques to accelerate the development of agents that modulate the function of a wide array of potential therapeutic targets. These targets have been selected through consultations with investigators in the University System of Maryland and beyond. A significant fraction of the Structural Biology portfolio arose via my association with the University of Maryland Marlene and Stewart Greenebaum Cancer Center and thus entails an effort to develop both research tools that will help us understand the root causes of various cancers and therapeutics that will combat those diseases. In this capacity, I am engaged in both smaller scale collaborations aimed at augmenting the research programs of other investigators and a research program that I direct. In the context of these two types of initiatives, my research has three main foci: (1) Structure-based drug design; (2); Neurological diseases involving the kynurenine pathway of tryptophan degradation; and (3) Oxidative DNA damage repair.
therapeutic development, X-ray crystallography, neurodegeneration, DNA repair
Pidugu, L.S., Mbimba, J.C.E., Ahmad, M., Pozharski, E., Sausville, E.A., Emadi, A., and Toth, E.A. (2016) A direct interaction between NQO1 and a chemotherapeutic dimeric naphthoquinone. BMC Structural Biology, 16(1): 1.
Cavalier, M.C., Ansari, M.I., Pierce, A.D., Wilder, P.T., McKnight, L.E., Rahman, E.P., Neau, D.B., Bezawada, P., Alasady, M.J., Varney, K.M., Toth, E.A., MacKerell, A.D., Coop, A. and Weber, D.J. (2016) Small Molecule Inhibitors of Ca2+-S100B Reveal Two Protein Conformations, Journal of Medicinal Chemistry, 59(2):592-608.
Malik, S.S., Patterson, D.N., Ncube, Z., and Toth, E.A. (2014) The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid. Proteins: Structure, Function, and Bioinformatics, 82(3): 405-14.
Luncsford, P.J., Manvilla, B.A., Patterson, D.N., Malik, S.S., Jin, J., Hwang, B-J., Gunther, R., Kalvakolanu, S., Lipinski, L.J., Yuan, W., Lu, W., Drohat, A.C., Lu, A-L., and Toth, E.A. (2013) Coordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions. DNA Repair, 12(12), 1043-52.