Publications

  • Rana, H., Moussatche, P., Rocha, L. S., Abdellaoui, S., Minteer, S. D., and Moomaw, E. W. (2016) Isothermal titration calorimetry uncovers substrate promiscuity of bicupin oxalate oxidase from Ceriporiopsis subvermispora, Biochemistry and Biophysics Reports 5, 396-400.

  • Liang, X., Moomaw, E., Rollins, J. (2015) Oxalate decarboxylase-mediated oxalate catabolism regulates compound appressorium development and infection inSclerotinia sclerotiorum. Molecular Plant Pathology, 16(8), 825-836.

  • Molina, L., Goodall, T., Twahir, U., Moomaw, E., Angerhofer, A. (2014) Real-Time kinetic studies of Bacillus subtilis oxalate decarboxylase and Cereporiopsis subvermispora oxalate oxidaseusing a luminescent oxygen sensor. Journal of Biochemical Technology, 5(4), 826-831. http://www.jbiochemtech.com/index.php/jbt/article/view/JBT5410

  • Moomaw, E.W., Uberto, R., and Tu, C.K. (2014) Membrane Inlet Mass Spectrometry Reveals that Ceriporiopsis subvermispora Bicupin Oxalate Oxidase is Inhibited by Nitric Oxide, Biochemical and Biophysical Research Communications, 450(1), 750- 754. doi:10.1016/j.bbrc.2014.06.040.

  • Uberto, R. and Moomaw, E.W. (2013) Protein Similarity Networks Reveal Relationships Among Sequence, Structure, and Function Within the Cupin Superfamily, PLoS ONE 8(9): e74477. doi:10.1371/journal.pone.0074477.
  • Moomaw, E.W., Hoffer, E., Moussatche, P., Salerno, J.C., Grant M, Immelman, B., Uberto, R., Ozarowski, A., Angerhofer, A. (2013) Kinetic and Spectroscopic Studies of Bicupin Oxalate Oxidase and Putative Active Site Mutants. PLoS ONE 8(3): e57933. doi:10.1371/journal.pone.0057933.
  • Moussatche, P., Angerhofer,A., Imaram, W., Hoffer, E., Uberto, K. , Brooks, C., Bruce, C., Sledge, D., Richards, N. G.  J., Moomaw, E. W.  (2011) Characterization of Ceriporiopsis subvermispora Bicupin Oxalate Oxidase Expressed In Pichia pastoris. Archives of Biochemistry and Biophysics 509, 100-107.
  • Moomaw, E. W., Angerhofer, A., Moussatche, P., Ozarowski, A., Garcia-Rubio, I., Richards, N.G.J. (2009): Metal Dependence of Oxalate Decarboxylase Activity. Biochemistry 48, 6116–6125.
  • Angerhofer, A., Moomaw, E. W., Garcia-Rubio, I., Ozarowski, A., Krzystek, J., Weber, R. T. and Richards, N. G. (2007) Multifrequency EPR Studies on the Mn(II) Centers of Oxalate Decarboxylase, J Phys Chem B 111, 5043-5046.
  • Love, R.A., Parge, H.A., Wickersham, J.A., Hostomsky, Z., Habuka, N., Moomaw, E.W., Adachi, T., Margosiak, S., Dagostino, E., Hostomska, Z. (1998): Conformational Changes in hepatitis C virus NS3 proteinase during NS4A complexation: correlation with enhanced cleavage and implications for inhibitor design. Therapies for Viral Hepatitis, Edited by R.F. Schinazi, J-P Sommadossi and H.C. Thomas, 1998: 247-254.
  • Love, R.A., Parge, H.A., Wickersham, J.A., Hostomsky, Z., Habuka, N., Moomaw, E.W., Adachi, T., Hostomska, Z., (1996): The Crystal Structure of Hepatitis C Virus NS3 Protease Reveals a Trypsin-like Fold and a Structural Zinc Binding Site. Cell, 87, 331-342.
  • Jones, T. R., et al., (1996) Structure-based design of lipophilic quinazoline inhibitors of thymidylate synthase. J. Med. Chem. 39, 904-917.
  • Dragovich, P. S., et al., (1996) Structure-based design of novel, urea-containing FKBP12 inhibitors. J. Med. Chem. 39, 1872-1884.
  • Menge, K.L., Hostomsky, Z., Nodes, B.R., Hudson, G.O., Rahmati, S., Moomaw, E.W., Almassy, R.J. and Hostomska, Z. (1995): Structure-Function Analysis of the Mammalian DNA Polymerase b Active Site: Role of Aspartic Acid 256, Arginine 254, and Arginine 258 in Nucleotidyl Transfer. Biochemistry, 34, 15934-15942.
  • Babine, R.E., Bleckman, T.M., Kissinger, C.R., Showalter, R., Pelletier, L.A., Lewis, C., Tucker, K., Moomaw, E., Parge, H.E., and Villafranca, J.E. (1995): Design, Synthesis and X-ray Crystallographic Studies of Novel FKBP-12 Ligands. Bioorganic & Medicinal Chemistry Letters, 5, 1719-1724.
  • Kissinger, C.R., Parge, H.E., Knighton. D.R., Lewis, C.T., Pelletier, L.A., Tempczyk, A., Kalish, V.J., Tucker, K.D., Showalter., R.E., Moomaw, E.W., Gastinel, L.N., Habuka, N., Chen, X., Maldonaldo, F., Barker, J.E., Bacquet, R. and Villafranca, E. (1995) : Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature 378, 641-644.
  • Hostomsky, Z., Hostomska, Z., Hudson, G.O., Moomaw, E.W., and Nodes, B.R. (1991) Reconstitution in vitro of RNase H Activity By Using N-Terminal and C-Terminal Domains of Human Immuno-defiiciency Virus Type I Reverse Transcriptase. Proc. Natl. Acad. Sci. USA 88, 1148-1152.
  • Appelt, K, et al., (1991) Design of Enzyme Inhibitors Using Iterative Protein Crystallographic Analysis. J. Med. Chem.34, 1925-1934.
  • Jablonski, E., Moomaw, E.W., Tullis, R.H. and Ruth, J.L. (1986): Preparation of Oligodeoxynucleotide-Alkaline Phosphatase Conjugates and their Use as Hybridization Probes. Nucl. Acids Res. 14, 6115-6128.
  • Hairfield, E.M., Moomaw, E.W., Tamburri, R.A., and Vigil, R.A. (1985): The Epoxidation of 2,5-Di-tert-butyl-1,4-benzoquinone, A Consecutive Reaction for the Physical Chemistry Laboratory. J. Chem. Ed. 62, 175-177.
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