Structure-function relationships in the Na,K-ATPase a subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme

Structure-function relationships in the Na,K-ATPase alpha subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme. Biochemistry 27(22): 8400-8408, 1988

Random mutagenesis of the sheep sodium, potassium-ATPase alpha subunit generates a ouabain resistant enzyme. FASEB Journal 7(3-4): A816, 1993

Random mutagenesis of the sheep Na,K-ATPase a-1 subunit generates a novel T797N mutation that results in a ouabain-resistant enzyme. The Journal of Biological Chemistry 268: 632-5, 1993

Random mutagenesis of the sheep Na,K-ATPase alpha-1 subunit generates a novel T797N mutation that results in a ouabain-resistant enzyme. Journal of Biological Chemistry 268(34): 25632-25635, 1993

Site-directed mutagenesis of a conserved, extracellular aspartic acid residue affects the ouabain sensitivity of sheep Na,K-ATPase. Journal of Biological Chemistry 264(36): 21902-21906, 1989

The phosphorylation site of the Kdp-ATPase of Escherichia coli: Site-directed mutagenesis of the aspartic acid residues 300 and 307 of the KdpB subunit. Molecular Microbiology 6(23): 3511-3520, 1992

Site directed mutagenesis of a conserved extracellular aspartic acid residue affects the ouabain sensitivity of sheep sodium potassium atpase. Journal of Biological Chemistry 264(36): 21902-21906, 1989

Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. Journal of Biological Chemistry 266(24): 15938-15943, 1991

Structure-function studies of Na,K-ATPase. Site-directed mutagenesis of the border residues from the H1-H2 extracellular domain of the a subunit. The Journal of Biological Chemistry 265: 38-41, 1990

Structure-function studies of Na,K-ATPase. Site-directed mutagenesis of the border residues from the H1-H2 extracellular domain of the alpha subunit. Journal of Biological Chemistry 265(12): 6638-6641, 1990

Site directed mutagenesis of active site residues in the alpha subunit of tryptophan synthase from salmonella typhimurium single site and double site replacements of aspartic acid 60 tyrosine 175 and glycine 211. Journal of Cell Biology 107(6 Part 3): 226A, 1988

Site-directed mutagenesis of the arginine-glycine-aspartic acid in vitronectin abolishes cell adhesion. Journal of Biological Chemistry 268(13): 9725-9729, 1993

Cys Site-Directed Mutagenesis of the Human SLC1A5 (ASCT2) Transporter: Structure/Function Relationships and Crucial Role of Cys467 for Redox Sensing and Glutamine Transport. International Journal of Molecular Sciences 19(3), 2018

Site-directed mutagenesis of aspartic acid 372 at the ATP binding site of yeast phosphoglycerate kinase: over-expression and characterization of the mutant enzyme. Protein Engineering 3(6): 515-521, 1990

Site-directed mutagenesis of the arginine-glycine-aspartic acid sequence in osteopontin destroys cell adhesion and migration functions. Journal of Cellular Biochemistry 57(4): 680-690, 1995