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Byers Larry D.
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http://hub.abes.fr/acs/periodical/joceah/1992/volume_57/issue_25/101021jo00051a026/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/1981/volume_103/issue_20/101021ja00410a032/authorship/2
http://hub.abes.fr/acs/periodical/jmcmar/1998/volume_41/issue_25/101021jm980146x/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1973/volume_12/issue_11/101021bi00735a008/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1975/volume_14/issue_16/101021bi00687a023/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1975/volume_14/issue_25/101021bi00696a008/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/1979/volume_101/issue_11/101021ja00505a030/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_35/101021ja993341p/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1986/volume_25/issue_9/101021bi00357a036/authorship/4
http://hub.abes.fr/acs/periodical/joceah/1988/volume_53/issue_16/101021jo00251a041/authorship/2
http://hub.abes.fr/acs/periodical/joceah/1989/volume_54/issue_22/101021jo00283a015/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1979/volume_18/issue_12/101021bi00579a006/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1985/volume_24/issue_14/101021bi00335a022/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1973/volume_12/issue_18/101021bi00742a602/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1979/volume_18/issue_20/101021bi00587a017/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/1981/volume_103/issue_20/101021ja00410a033/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/1977/volume_99/issue_12/101021ja00454a039/authorship/1
http://hub.abes.fr/acs/periodical/jacsat/1992/volume_114/issue_14/101021ja00040a011/authorship/2
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Methylimidazole-catalyzed ester hydrolysis: nonlinear kinetics
Interaction of phosphate analogs with glyceraldehyde-3-phosphate dehydrogenase
Corrections - Binding of the By-Product Analog Benzylsuccinin Acid by Carboxypeptidase A.
Specificity of induced conformational changes. Case of yeast glyceraldehyde-3-phosphate dehydrogenase
.beta.-Glucosidase: substrate, solvent, and viscosity variation as probes of the rate-limiting steps
Acyl substituent effects on thiohemiacetal equilibriums
Criteria for evaluating enzymic rate enhancements. The case of glyceraldehyde-3-phosphate dehydrogenase
Interaction of the substrate phosphate substituent with glyceraldehyde-3-phosphate dehydrogenase
Binding of the by-product analog benzylsuccinic acid by carboxypeptidase A
An Assessment of Desolvation on Rates of Acetyl Transfer: Insightsinto Enzyme Catalysis
Structure−Activity Relationships for Antiplasmodial Activity among7-Substituted 4-Aminoquinolines
The remarkable nucleophilic reactivity of molybdate
Reversible inhibitors of .beta.-glucosidase
Nucleophilic reactions of molybdate
Effect of phosphono substituents on acyl transfer reactions
Acyl substituent effects on rates of acyl transfer to thiolate, hydroxide, and oxy dianions
Acyl substituent effects on ester aminolysis
Subunit interactions in yeast glyceraldehyde-3-phosphate dehydrogenase
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