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Science (New York, N.Y.)|August 31, 1990
Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenaseA M Dean, D E KoshlandStructure (London, England : 1993)|November 15, 1994
Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificityJ H Hurley, A M DeanProtein Science : a Publication of the Protein Society|May 25, 1999
Carbocations in the synthesis of prostaglandins by the cyclooxygenase of PGH synthase? A radical departure!A M Dean, F M DeanAnnual Review of Genetics|November 28, 2000
Molecular-functional studies of adaptive genetic variation in prokaryotes and eukaryotesW B Watt, A M DeanTrends in Ecology & Evolution|January 15, 2011
Enzyme activity and fitness: Evolution in solutionD E Dykhuizen, A M DeanProceedings of the National Academy of Sciences of the United States of America|December 5, 1995
A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificityR Chen, A Greer, A M DeanProceedings of the National Academy of Sciences of the United States of America|October 29, 1996
Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenaseR Chen, A Greer, A M DeanBiochemistry|May 7, 1996
Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ --> NAD+ specificity-reversal mutantJ H Hurley, R Chen, A M DeanEuropean Journal of Biochemistry|January 15, 1998
Structural constraints in protein engineering--the coenzyme specificity of Escherichia coli isocitrate dehydrogenaseR Chen, A F Greer, A M DeanProceedings of the National Academy of Sciences of the United States of America|May 11, 2000
Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolutionJ G Bishop, A M Dean, T Mitchell-OldsPageof 7