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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
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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
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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
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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)
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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
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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
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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).
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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
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Wood, Z.A., Sabatini, R.S. and Hajduk, S.L. RNA ligase: Picking up the pieces. Molecular Cell (2004) 13, 455-6
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Wood, Z.A., Poole, L.B. and Karplus, P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science (2003) 300, 650-3
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Wood, Z.A., Schroder, E, Harris, J.R and Poole, L.B. Structure, mechanism and regulation of peroxiredoxins. TiBS (2003) 28, 32-40.
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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
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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)
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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
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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
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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
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Priest, J.W., Wood, Z.A., and Hajduk, S.L. Cytochromes c1of kinetoplastid protozoa lack mitochondrial targeting presequences. Biochemica et Biophysica Acta (1993) 1144, 229-231
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Hajduk, S.L., Adler, B., Bertrand, K., Fearon, K., Hager, K., Hancock, K., Harris, M., LeBlanc, A., Moore, R., Pollard, V., Priest, J., and Wood, Z.A. (1992) Molecular Biology of African Trypanosomes: Development of new strategies to combat an old disease. American Journal for the Medical Sciences 303, 258-269