Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable ProbeACCOUNTS OF CHEMICAL RESEARCHIF17.72021-05-0310OAAI
Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic ReactionsJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62021-02-0914OAAI
Uncovering the Role of Key Active-Site Side Chains in Catalysis: An Extended Bronsted Relationship for Substrate Deprotonation Catalyzed by Wild-Type and Variants of Triosephosphate IsomeraseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62019-09-1116OAAI
Role of the Carboxylate in Enzyme-Catalyzed Decarboxylation of Orotidine 5′-Monophosphate: Transition State Stabilization Dominates Over Ground State DestabilizationJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62019-07-3110OAAI
Enzyme Architecture: Breaking Down the Catalytic Cage that Activates Orotidine 5′-Monophosphate Decarboxylase for CatalysisJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62018-11-2614OAAI
Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate IsomeraseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62018-06-0426OAAI
Orotidine 5′-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme CatalysisACCOUNTS OF CHEMICAL RESEARCHIF17.72018-03-2936OAAI
Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate IsomeraseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62018-03-0829OAAI
Enzyme Architecture: Erection of Active Orotidine 5'-Monophosphate Decarboxylase by Substrate-Induced Conformational Changes酶结构: 通过底物诱导的构象变化使活性的Orotidine 5'-单磷酸脱羧酶勃起JOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62017-10-2316OAAI
Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate IsomeraseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62017-07-1944OAAI
Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride TransferJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62016-11-1024OAAI
Structure-Reactivity Effects on Intrinsic Primary Kinetic Isotope Effects for Hydride Transfer Catalyzed by Glycerol-3-phosphate DehydrogenaseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62016-10-2713OAAI
Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate IsomeraseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62015-11-3037OAAI
Enzyme Architecture: Optimization of Transition State Stabilization from a Cation-Phosphodianion PairJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62015-04-2132OAAI
The Activating Oxydianion Binding Domain for Enzyme-Catalyzed Proton Transfer, Hydride Transfer, and Decarboxylation: Specificity and Enzyme ArchitectureJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62015-01-2051OAAI
Enzyme architecture: on the importance of being in a protein cageCURRENT OPINION IN CHEMICAL BIOLOGYIF6.12014-08-01102OAAI
Enzyme Architecture: Deconstruction of the Enzyme-Activating Phosphodianion Interactions of Orotidine 5′-Monophosphate DecarboxylaseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62014-07-0236OAAI
Enzyme Architecture: Remarkably Similar Transition States for Triosephosphate Isomerase-Catalyzed Reactions of the Whole Substrate and the Substrate in PiecesJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62014-03-0634OAAI
Enzyme Architecture: The Activating Oxydianion Binding Domain for Orotidine 5′-Monophophate DecarboxylaseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62013-11-2718OAAI
Magnitude and Origin of the Enhanced Basicity of the Catalytic Glutamate of Triosephosphate IsomeraseJOURNAL OF THE AMERICAN CHEMICAL SOCIETYIF15.62013-04-1043OA
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