Long-range structural effects in a second-site revertant of a mutant dihydrofolate reductase.
Proc.Natl.Acad.Sci.USA (1993)
;How Do Mutation at Phenylalanine-153 and Isoleucine-155 Partially Suppress the Effects of the Aspartate-27-> Serine Mutation in Escherichia Coli Dihydrofolate Reductase
;
Biochemistry (1993)
;Role of Aspartate 27 of Dihydrofolate Reductase from Escherichia Coli in Interconversion of Active and Inactive Enzyme Conformers and the Binding of Nadph
;
J.Biol.Chem. (1990)
;A Second-Site Mutation at Phenylalanine-137 that Increases Catalytic Efficiency in the Mutant Aspartate-27-> Serine Escherichia Coli Dihydrofolate Reductase
;
Biochemistry (1990)
;Dihydrofolate Reductase from Escherichia Coli: Probing the Role of Aspartate-27 and Phenylalanine-137 in Enzyme Conformation and the Binding of Nadph
;
Biochemistry (1990)
Functional Role of Aspartic Acid-27 in Dihydrofolate Reductase Revealed by Mutagenesis
Science (1986)
;Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase at 1.7 Angstroms Resolution. I. General Features and Binding of Methotrexate
;
Biochemistry (1982)
;Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase at 1.7 Angstroms Resolution. II. Environment of Bound Nadph and Implications for Catalysis
;
J.Biol.Chem. (1982)