Journal article
Authors list: Kanzok, SM; Fechner, A; Bauer, H; Ulschmid, JK; Müller, HM; Botella-Munoz, J; Schneuwly, S; Schirmer, RH; Becker, K
Publication year: 2001
Pages: 643-646
Journal: Science
Volume number: 291
Issue number: 5504
ISSN: 0036-8075
eISSN: 1095-9203
DOI Link: https://doi.org/10.1126/science.291.5504.643
Publisher: American Association for the Advancement of Science
Abstract:
The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage. Here we demonstrate the absence of glutathione reductase in Drosophila melanogaster, identify a new type of thioredoxin reductase, and provide evidence that a thioredoxin system supports GSSG reduction. Our data suggest that antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.
Citation Styles
Harvard Citation style: Kanzok, S., Fechner, A., Bauer, H., Ulschmid, J., Müller, H., Botella-Munoz, J., et al. (2001) Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster, Science, 291(5504), pp. 643-646. https://doi.org/10.1126/science.291.5504.643
APA Citation style: Kanzok, S., Fechner, A., Bauer, H., Ulschmid, J., Müller, H., Botella-Munoz, J., Schneuwly, S., Schirmer, R., & Becker, K. (2001). Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science. 291(5504), 643-646. https://doi.org/10.1126/science.291.5504.643