Wood, Zachary - The University of Georgia - Department of Biochemistry & Molecular Biology

个人简介

Cornell University, Ph.D., Biochemistry University of Alabama (Birmingham), B.S., Chemistry

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Sanchez, J.E., Gross, P.G., Goetze, R., Walsh, R., Jr., Peeples, W.J. and Wood, Z.A. Evidence of kinetic cooperativity in dimeric ketopantoate reductase from Staphylococcus Aureus. Biochemistry (2015) 54, 21, p3360 Walsh, R., Jr., Polizzi, S.J., Kadirvelraj, R., Howard, W. and Wood, Z.A. Man o’ War Mutation in UDP-α-D-Xylose Synthase Favors the Abortive Catalytic Cycle and Uncovers a Latent Potential for Hexamer Formation. Biochemistry (2015) 54, 3, p807 Kadirvelraj, R., Custer, G.C., Keul, N.C., Sennet, N.C., Sidlo, A.M., Walsh, R., Jr. and Wood, Z.A. Hysteresis in Human UDP-Glucose Dehydrogenase Is Due to a Restrained Hexameric Structure That Favors Feedback Inhibition Biochemistry (2014) 53, 51, p8043 Polizzi, S.J., Walsh, R., Jr., Le Magueres, P. Criswell, A.R. and Wood, Z.A. Human UDP-xylose synthase forms a high activity tetramer. Biochemistry (2013) 52, 22, p3888. Kadirvelraj, R., Custer, G.C., Sennet, N.C., and Wood, Z.A. Hysteresis and negative cooperativity in human UDP-Glucose Dehydrogenase. Biochemistry (2013) 52, 8, p1456. Oruganty, K., Talathi, N.S., Wood, Z.A., and Kannan, N. Identification of a hidden strain "switch" provides clues to an ancient structural mechanism in protein kinases PNAS (2013) 110, 3, p924. Polizzi, S.J., Walsh, R., Jr., Peeples, W.B., Lim, J., Wells, L. and Wood, Z.A. Human UDP-xylose synthase and E. coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced. Biochemistry (2012) 51, 44, p8844. Sennet, N.C., Kadirvelraj, R. and Wood, Z.A. Cofactor binding triggers a molecular switch to allosterically activate human UDP-Glucose Dehydrogenase. Biochemistry (2012) 51, 46, p9364. Sennet, N.C., Kadirvelraj, R. and Wood, Z.A. Conformational flexibility in the allosteric regulation of human UDP-Glucose Dehydrogenase. Biochemistry (2011) 50, 44, p9651. Kadirvelraj, R. Sennet, N.C., Polizzi, S.J., Weitzel, S., Wood, Z.A. The role of packing defects in the evolution of allostery and induced fit in human UDP-Glucose Dehydrogenase. Biochemistry (2011) 50, 25, p5780. Eames, B.F., Singer, A., Smith, G., Wood. Z.A., Yan, Yi-Lin, He, X., Polizzi, S.J., and Postlethwait, J.H. UDP-xylose synthase 1 is required for morphogenesis and histogenesis of the craniofacial skeleton. Developmental Biology (2010) 15, 341, p400. Ochsenreiter, T., Anderson, S., Wood, Z.A. and Hajduk, S.L. Alternative editing produces a novel protein involved in mitochondrial DNA maintenance in trypanosomes. Mol. Cell. Biol. (2008) 28, 5595-604. Wood, Z.A., Weaver, L.H., Brown, P.H., Beckett, D. and Matthews, B.W. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. Journal of Molecular Biology (2006) 357 509-23 (Cover Illustration) Parsonage, D., Youngblood, D.S., Sarma, G.N., Wood, Z.A., Karplus, P.A., and Poole, L.B. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry (2005), 44, 10583-92 Roberts, B.A., Wood, Z.A., Jönsson, T.J., Poole, L.B., and Karplus, P.A. Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF. Protein Science (2005) 14, 2414-20 Poole, L.B. Roberts, B.A., Wood, Z.A., Jönsson, T.J., Reynolds, C.M., and Karplus, P.A. The AhpC-Reducing, Thioredoxin-Like N-Terminal Domain of AhpF. Flavins and Flavoproteins (2005). He, M.M., Wood, Z.A., Baase, W.A., Xiao, H. and Matthews, B.W. Alanine-scanning mutagenesis of phage T-4 lysozyme suggests that tertiary context has a dominant effect on b-sheet formation. Protein Science (2004) 13, 2716-24 Wood, Z.A., Sabatini, R.S. and Hajduk, S.L. RNA ligase: Picking up the pieces. Molecular Cell (2004) 13, 455-6 Wood, Z.A., Poole, L.B. and Karplus, P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science (2003) 300, 650-3 Wood, Z.A., Schroder, E, Harris, J.R and Poole, L.B. Structure, mechanism and regulation of peroxiredoxins. TiBS (2003) 28, 32-40. Wood, Z.A., Poole, L. B., Hantgan, R.R. and Karplus, P. A. Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry (2002) 41, 5493-5504 Wood, Z.A., Poole, L. B., and Karplus, P. A. Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis. Biochemistry (2001) 40, 3900-3911 (Journal Cover from 7/02 to 9/02) Poole, L. B., Reynolds, C. M., Wood, Z.A., Karplus, P. A., Ellis, H. R., and Li Calzi, M. AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Eur J Biochem (2000) 267, 6126-33 Rodriguez, E, Wood, Z.A., Karplus, P. A., and Lei, X. G. Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris. Arch Biochem Biophys (2000) 382, 105-112 Sprous, D., Zacharias, W., Wood, Z.A., and Harvey, S.C. Dehydrating agents sharply reduce curvature in DNAs containing A tracts. Nucleic Acids Research (1995) 23, 1816-21