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Chemistry (Weinheim an Der Bergstrasse, Germany)|March 14, 2020
Through the Looking Glass: Chiral Recognition of Substrates and Products at the Active Sites of Racemases and EpimerasesStephen L BearneMethods in Enzymology|October 20, 2023
Design and evaluation of substrate-product analog inhibitors for racemases and epimerases utilizing a 1,1-proton transfer mechanismStephen L BearneBioessays : News and Reviews in Molecular, Cellular and Developmental Biology|July 8, 2024
Biochemical communication between filament-forming enzymes: Potential Regulatory Roles of Metabolites in Enzyme Co-assemblies with CTP SynthaseStephen L BearnePhilosophical Transactions of the Royal Society of London. Series B, Biological Sciences|January 12, 2023
Capturing the free energy of transition state stabilization: insights from the inhibition of mandelate racemaseStephen L BearneOrganic & Biomolecular Chemistry|July 19, 2019
The role of Brønsted base basicity in estimating carbon acidity at enzyme active sites: a caveatStephen L BearneBiochimica Et Biophysica Acta. Proteins and Proteomics|February 10, 2017
The interdigitating loop of the enolase superfamily as a specificity binding determinant or 'flying buttress'Stephen L BearneBiochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|October 21, 2025
A practical consideration for the substrate concentration when determining IC<sub>50</sub> values for enzyme inhibitionStephen L BearneOrganic & Biomolecular Chemistry|October 31, 2014
Synthesis of coenzyme A thioesters using methyl acyl phosphates in an aqueous mediumMohan Pal, Stephen L BearneThe Biochemical Journal|October 18, 2002
Aspartate-107 and leucine-109 facilitate efficient coupling of glutamine hydrolysis to CTP synthesis by Escherichia coli CTP synthaseAkshai Iyengar, Stephen L BearneBioorganic & Medicinal Chemistry Letters|February 11, 2014
Inhibition of glutamate racemase by substrate-product analoguesMohan Pal, Stephen L BearnePageof 8