Time Evolution of the Quaternary Structure of Escherichia Coli Aspartate Transcarbamoylase Upon Reaction With the Natural Substrates And a Slow Tight Binding Inhibitor von West, J.M., Xia, J., Tsuruta, H., Guo, W., O'Day, E.M., Kantrowitz, E.R.

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Pyrococcus abyssi alkaline phosphatase: the dimer is the active form von Zappa, S., Boudrant, J., Kantrowitz, E.R.

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Replacement of Asp‐162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylas... von Fetler, L., Tauc, P., Baker, D.P., Macol, C.P., Kantrowitz, E.R., Vachette, P.

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Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphatase von Murphy, J E, Xu, X, Kantrowitz, E R

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Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition von Giroux, E, Williams, M K, Kantrowitz, E R

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The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites von Zhang, Y, Kantrowitz, E R

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Importance of the dimer-dimer interface for allosteric signal transduction and AMP cooperativity of pig kidney fructose-1,6-bisphosphatase: site-specific mutagenesis studies of GLU... von Lu, G.Q. (Boston College, Chesnut Hill, MA.), Giroux, E.L, Kantrowitz, E.R

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The importance of aspartate 327 for catalysis and zinc binding in Escherichia coli alkaline phosphatase von Xu, X, Kantrowitz, E R

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The Ala-161→Thr Substitution in Escherichia coli Alkaline Phosphatase Does Not Result in Loss of Enzymatic Activity Although the Homologous Mutation in Humans Causes Hypophosphatas... von Chaidaroglou, A., Kantrowitz, E.R.

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Alteration of aspartate 101 in the active site of Escherichia coli alkaline phosphatase enhances the catalytic activity von Chaidaroglou, Antigoni, Kantrowitz, Evan R.

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Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization... von Baker, D P, Stebbins, J W, DeSena, E, Kantrowitz, E R

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Overexpression and Purification of the Trimeric Aspartate Transcarbamoylase from Bacillus subtilis von Baker, D.P., Aucoin, J.M., Williams, M.K., Demello, L.A., Kantrowitz, E.R.

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Structural consequences of a one atom mutation on aspartate transcarbamylase from E. coli von Cherfils, J., Sweet, R.M., Middleton, S.A., Kantrowitz, E.R., Tauc, P., Vachette, P.

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An essential arginine residue in porcine phospholipiase A2 von Vensel, L A, Kantrowitz, E R

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The role of tryptophan in aspartate transcarbamylase von Foote, J, Ikeda, D M, Kantrowitz, E R

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The interaction of tetraiodofluorescein with aspartate transcarbamylase von Jacobsberg, L.B., Kantrowitz, E.R., McMurray, C.H., Lipscomb, W.N.

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