Although PARK7 has beenwidely studied for more than two decadesbecause of its multifunctional roles and its link to both cancer andneurodegenerative diseases, potent and selective PARK7 inhibitorsare remarkably scarce.22−25 Recently, the level of PARK7 has been shown to be downregulatedby several anticancer drug candidates.26−28 However, it is stillobscure whether the effect of PARK7 downregulation by these drugsis due to the scaffolding function of the full-length protein or itscatalytic activity regulated by the highly conserved cysteine residueCys106. The gene discussed is PARK7; the disease is glycogen storage disease VI.