The role of active-site residues Phe98, HiS239, and Arg243 in DNA binding and in the catalysis of human uracil–DNA glycosylase SMUG1

Research output: Contribution to journal › Article › peer-review

DNA repair, Fluorescence, Homology modeling, Human uracil–DNA glycosylase, Molecular dynamics simulation, Mutant, SMUG1, Stopped-flow kinetics, Structure, DOMAIN, molecular dynamics simulation, THYMINE, REPAIR, homology modeling, fluorescence, STRUCTURAL BASIS, EXCISION, human uracil-DNA glycosylase, SPECIFICITY, structure, DAMAGE-RECOGNITION, 5-HYDROXYMETHYLURACIL, ENZYME, stopped-flow kinetics, mutant, PROTEINS

ID: 21346256