Toth, Eric A. - University of Maryland-Baltimore - Department of Biochemistry and Molecular Biology

个人简介

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 and co-Director of the Structural Biology Shared Service. As such, I collaborate with both basic and clinical research investigators to study the basic mechanisms of cancer development and metastasis and to identify candidate proteins that may serve as targets for therapeutic intervention.

研究领域

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 agenst 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) Oxidative DNA damage repair; and (3) Neurological diseases involving the kynurenine pathway of tryptophan degradation.

近期论文

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Cavalier MC, Pierce AD, Wilder PT, Alasady MJ, Hartman KG, Neau DB, Foley TL, Jadhav A, Maloney DJ, Simeonov A, Toth EA, Weber DJ. (2014) Covalent Small Molecule Inhibitors of Ca(2+)-Bound S100B. Biochemistry, 53(42): 6628-40. Jin, J., Hwang, B-J., Chang, P-W., Toth, E.A., and Lu, A-L. (2014) Interactions of apurinic/apyrimidinic endonuclease 2 (Apn2) with Myh1 DNA glycosylase in fission yeast DNA Repair. DNA Repair, 15(1): 1-10. 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. Manvilla, B.A., Pozharski, E., Toth, E.A., and Drohat, A.C. (2013) Crystal structure of human apurinic/apyrimidinic endonuclease 1 with the essential Mg2+ cofactor. Acta Crystallographica D69, 2555-62. 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. Pazgier M, Ericksen B, Ling M, Toth EA, Shi J, Li X, Galliher-Beckley A, Lan L, Zou G, Zhan C, Yuan W, Pozharski E, Lu W. (2013) Structural and functional analysis of the pro-domain of human cathelicidin, LL-37. Biochemistry, 52(9): 1547-58. Erzurumlu, Y., Kose, F.A., Gozen, O., Gozuacik, D., Toth, E.A., Ballar, P. (2013) A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization. Int. J. Biochem. & Cell Biol., 45(4): 773-82. Kishor A, Tandukar B, Ly YV, Toth EA, Suarez Y, Brewer G, Wilson GM. (2013) Hsp70 is a novel posttranscriptional regulator of gene expression that binds and stabilizes selected mRNAs containing AU-rich elements. Mol. Cell. Biol., 33(1): 71-84. McKnight, L. E., Raman, E.P., Bezawada, P., Kudrimoti, S., Wilder, P.T., Hartman, K.G., Godoy-Ruiz, R., Toth, E.A., Coop, A., MacKerell, A.D. and Weber, D.J. (2012) Structure-Based Discovery of a Novel Pentamidine-Related Inhibitor of the Calcium-Binding Protein S100B. ACS Med. Chem. Lett., 3(12): 975-9. Liriano MA, Varney KM, Wright NT, Hoffman CL, Toth EA, Ishima R, Weber DJ. (2012) Target Binding to S100B Reduces Dynamic Properties and Increases Ca(2+)-Binding Affinity for Wild Type and EF-Hand Mutant Proteins. J. Mol. Biol., 423(3):365-85 Manvilla, BA, Maiti, A, Begley, MC, Toth, EA, and Drohat, AC. (2012) Crystal structure of human methyl-binding domain IV glycosylase bound to abasic DNA. J Mol. Biol., 420(3), 164-75. Bernstein, J. and Toth, E.A. (2012) Yeast Nuclear RNA Processing. World J. Biol. Chem., 3(1), 7-26. Luncsford, P.J., Chang, D-Y., Shi, G., Bernstein, J., Madabushi, A., Patterson, D.N., Lu, A-L., and Toth, E.A. (2010) A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions. J. Mol. Biol., 403(3), 351-370. PMCID: PMC2953589. Zucconi BE, Ballin JD, Brewer BY, Ross CR, Huang J, Toth EA, Wilson GM. (2010) Alternatively expressed domains of AU-rich element RNA- binding protein 1 (AUF1) regulate RNA-binding affinity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands. J. Biol. Chem., 285(50), 39127-39. PMCID: PMC2998080. Ballin, J.D., Prevas, J.P., Ross, C.R., Toth, E.A., Wilson, G.M., Record M.T. (2010). Contributions of the histidine side chain and the N-terminal alpha-amino group to the binding thermodynamics of oligopeptides to nucleic acids as a function of pH. Biochemistry, 49, 2018-2030. PMCID: PMC2864607 Bernstein J, Ballin JD, Patterson DN, Wilson GM, Toth EA. (2010). Unique properties of the Mtr4p-poly(A) complex suggest a role in substrate targeting. Biochemistry, 49(49),10357-70. PMCID: PMC2999651. Wilder, P.T., Charpentier, T.H., Liriano, M.A., Gianni, K., Varney, K.M., Pozharski, E., Coop, A., Toth, E.A., MacKerell, A.D., and Weber, D.J. (2010) In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction. Int. J. High Throughput Screening, 2010(1), 109-126. PMCID: PMC2995924. Charpentier, T.H., Thompson, L.E., Liriano, M.A., Varney, K.M., Wilder, P.T., Pozharski, E., Toth, E.A., and Weber, D.J. (2010). The effect of the CapZ peptide (TRTK-12) binding to Ca2+-S100B as examined by NMR and X-ray crystallography, J Mol Biol, 396, 1227-1243. PMCID: PMC2843395. Charpentier, T.H., Wilder, P.T., Liriano, M.A., Varney, K.M., Zhong, S., Coop, A., Pozharski, E., MacKerell, A.D., Toth, E.A., and Weber, D.J. (2009). Small molecules bound to unique sites in the target protein binding cleft of calcium-bound S100B as characterized by nuclear magnetic resonance (NMR) and X-ray crystallography. Biochemistry, 48, 6202-6212. PMCID: PMC2804263. Charpentier, T.H., Wilder, P.T., Liriano, M., Varney, K.M., Pozharski, E., MacKerell, A.D., Coop, A., Toth, E.A., and Weber, D.J. (2008) Divalent metal ion complexes of S100B in the absence and presence of pentamidine. J Mol Biol, 382, 56-73. PMCID: PMC2636698.