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http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_1/101021bi011410i/authorship/1
http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_46/101021ja002851c/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_22/101021bi020105/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_28/101021bi000818x/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_38/101021bi011189/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_12/101021bi011696r/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_32/101021bi000914y/authorship/1
http://hub.abes.fr/acs/periodical/achre4/2001/volume_34/issue_12/101021ar000058i/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_7/101021bi027083b/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/1999/volume_121/issue_32/101021ja991280p/authorship/2
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The Temperature Dependence of Enzyme RateEnhancements
Catalysis by Entropic Effects: The Action of Cytidine Deaminase on5,6-Dihydrocytidine
Contribution of Enzyme−Phosphoribosyl Contacts to Catalysis by Orotidine5‘-Phosphate Decarboxylase
15N Kinetic Isotope Effects on Uncatalyzed and Enzymatic Deamination ofCytidine
Determination of the Affinity of Each Component of a Composite QuaternaryTransition-State Analogue Complex of Creatine Kinase
The Rate of Spontaneous Decarboxylation of AminoAcids
The Depth of Chemical Time andthe Power of Enzymes asCatalysts
Generation of an Active Monomer of Rabbit Muscle Creatine Kinase bySite-Directed Mutagenesis: The Effect of Quaternary Structure on Catalysisand Stability
Temperature Effects on the Catalytic Efficiency, Rate Enhancement, and TransitionState Affinity of Cytidine Deaminase, and the Thermodynamic Consequences forCatalysis of Removing a Substrate “Anchor”
Site-Bound Water and the Shortcomings of a Less than Perfect Transition StateAnalogue
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