GSH is a key cellular antioxidant and plays a major role in the phase 2 metabolic clearance of electrophilic xenobiotics. The importance of the GSH pathway and enzymes that affect this delicate balance is gaining an increased level of attention in recent years. Although glutathione reductase has been an attractive target for many pharmaceuticals, there have been no successful glutathione reductase related therapeutic compounds created to date. In particular, glutathione reductase appears to be a good target for anti-malarials, as the glutathione reductase of the malaria parasite "Plasmodium falciparum" has a significantly different protein fold than that of mammalian glutathione reductase. By designing drugs specific to "p. falciparum" it may be possible to selectively induce oxidative stress in the parasite, while not affecting the host.