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Biochemistry|June 25, 1996
Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathwayG B Strambini, P Cioni, P F CookThe Journal of Clinical Investigation|October 1, 1977
Relationship between phosphaluria and acute hypercapnia in the ratR K Webb, P B Woodhall, C C Tisher, et al.Biochemistry|January 14, 1986
Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinucleotide-malic enzyme reaction from isotope effects and pH studiesD M Kiick, B G Harris, P F CookBiochemistry|July 25, 1989
Substrate activation by malate induced by oxalate in the Ascaris suum NAD-malic enzyme reactionS H Park, B G Harris, P F CookArchives of Biochemistry and Biophysics|December 1, 1992
Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarateC J Lai, B G Harris, P F CookThe Journal of Biological Chemistry|October 15, 1987
Kinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modificationG S Rao, B G Harris, P F CookBiochemistry|October 14, 1980
Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactionsP F Cook, J S Blanchard, W W ClelandBiochemistry|April 9, 1999
Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzymeW E Karsten, C C Hwang, P F CookBiochemistry|September 29, 1981
Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenaseC E Grimshaw, P F Cook, W W ClelandBiochemistry|April 30, 1996
Isotope partitioning with Ascaris suum phosphofructokinase is consistent with an ordered kinetic mechanismG E Gibson, B G Harris, P F CookPageof 14