https://www.selleckchem.com/pr....oducts/FK-506-(Tacro
Consistent with these observations, we found that stable expression of wild-type, but not catalytically inactive MUTYH, enhances MNNG cytotoxicity in Mutyh-/- MEFs, and that MUTYH expression enhances MNNG-induced genomic strand breaks. Taken together, these results suggest that MUTYH enhances the rapid accumulation of AP-site intermediates by interacting with APE1, implicating MUTYH as a factor that modulates the delicate process of base-excision repair independently of its glycosylase activity. Published under license by Th
Like
Comment
Share
