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Results: 1-12 |
Results: 12
The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study
Authors: Czyryca, PG Hengge, AC
Citation: Pg. Czyryca et Ac. Hengge, The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study, BBA-PROT ST, 1547(2), 2001, pp. 245-253
Isotope effects in the study of enzymatic phosphoryl transfer reactions
Authors: Hengge, AC
Citation: Ac. Hengge, Isotope effects in the study of enzymatic phosphoryl transfer reactions, FEBS LETTER, 501(2-3), 2001, pp. 99-102
Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase
Authors: Rigas, JD Hoff, RH Rice, AE Hengge, AC Denu, JM
Citation: Jd. Rigas et al., Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase, BIOCHEM, 40(14), 2001, pp. 4398-4406
Isotope effects and medium effects on sulfuryl transfer reactions
Authors: Hoff, RH Larsen, P Hengge, AC
Citation: Rh. Hoff et al., Isotope effects and medium effects on sulfuryl transfer reactions, J AM CHEM S, 123(38), 2001, pp. 9338-9344
Lanthanide catalyzed cyclization of uridine 3 '-p-nitrophenyl phosphate
Authors: Rishavy, MA Hengge, AC Cleland, WW
Citation: Ma. Rishavy et al., Lanthanide catalyzed cyclization of uridine 3 '-p-nitrophenyl phosphate, BIOORG CHEM, 28(5), 2000, pp. 283-292
Kinetic isotope effects and stereochemical studies on a ribonuclease model: Hydrolysis reactions of uridine 3 '-nitrophenyl phosphate
Authors: Hengge, AC Bruzik, KS Tobin, AE Cleland, WW Tsai, MD
Citation: Ac. Hengge et al., Kinetic isotope effects and stereochemical studies on a ribonuclease model: Hydrolysis reactions of uridine 3 '-nitrophenyl phosphate, BIOORG CHEM, 28(3), 2000, pp. 119-133
Mutation of Arg-166 of alkaline phosphatase alters the thio effect but notthe transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases
Authors: Holtz, KM Catrina, IE Hengge, AC Kantrowitz, ER
Citation: Km. Holtz et al., Mutation of Arg-166 of alkaline phosphatase alters the thio effect but notthe transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases, BIOCHEM, 39(31), 2000, pp. 9451-9458
Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia
Authors: Hoff, RH Hengge, AC Wu, L Keng, YF Zhang, ZY
Citation: Rh. Hoff et al., Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia, BIOCHEM, 39(1), 2000, pp. 46-54
Comparison of the reaction progress of calcineurin with Mn2+ and Mg2+
Authors: Martin, BL Jurado, LA Hengge, AC
Citation: Bl. Martin et al., Comparison of the reaction progress of calcineurin with Mn2+ and Mg2+, BIOCHEM, 38(11), 1999, pp. 3386-3392
Does positive charge at the active sites of phosphatases cause a change inmechanism? The effect of the conserved arginine on the transition state for phosphoryl transfer in the protein-tyrosine phosphatase from Yersinia
Authors: Hoff, RH Wu, L Zhou, B Zhang, ZY Hengge, AC
Citation: Rh. Hoff et al., Does positive charge at the active sites of phosphatases cause a change inmechanism? The effect of the conserved arginine on the transition state for phosphoryl transfer in the protein-tyrosine phosphatase from Yersinia, J AM CHEM S, 121(41), 1999, pp. 9514-9521
The transition state of the phosphoryl-transfer reaction catalyzed by the lambda Ser/Thr protein phosphatase
Authors: Hoff, RH Mertz, P Rusnak, F Hengge, AC
Citation: Rh. Hoff et al., The transition state of the phosphoryl-transfer reaction catalyzed by the lambda Ser/Thr protein phosphatase, J AM CHEM S, 121(27), 1999, pp. 6382-6390
Comparisons of phosphorothioate and phosphate monoester transfer reactions: Activation parameters, solvent effects, and the effect of metal ions
Authors: Catrina, IE Hengge, AC
Citation: Ie. Catrina et Ac. Hengge, Comparisons of phosphorothioate and phosphate monoester transfer reactions: Activation parameters, solvent effects, and the effect of metal ions, J AM CHEM S, 121(10), 1999, pp. 2156-2163
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