Mutagenesis of conserved residues in the phosphorylation domain of the yeast plasma membrane H⁺-ATPase. Effects on structure and function

Chemical Compounds

• Thr-Ala 71%
• Lys-Gln 68%
• Mutation 65%
• Polypeptide 64%
• Lys-Arg 59%
• Thr-Ser 55%
• Glycine Residue 52%
• Substitution Reaction 48%
• Plasma 47%
• Reaction Intermediate 40%
• Site-Directed Mutagenesis 40%
• Toxic 29%
• Heat 28%
• Binding Site 27%
• Phosphate 25%
• Resistance 24%
• Hydrolysis 23%
• Amount 16%
• pH Value 16%
• Acid 13%

Medicine & Life Sciences

• Proton-Translocating ATPases 100%
• Adenosine Triphosphatases 77%
• Mutagenesis 76%
• Yeasts 62%
• Cell Membrane 56%
• Phosphorylation 53%
• Secretory Vesicles 44%
• Vanadates 33%
• beta-aspartyl phosphate 26%
• Enzymes 21%
• Adenosine Triphosphate 20%
• P-type ATPases 19%
• Peptides 16%
• Insertional Mutagenesis 15%
• Heat-Shock Response 14%
• Amino Acid Substitution 14%
• Site-Directed Mutagenesis 13%
• Glycine 13%
• Hydrolysis 11%
• Phosphates 11%
• Binding Sites 9%
• Poisons 9%
• Mutation 7%
• Growth 6%