Special Issue "Peroxiredoxin"
A special issue of Antioxidants (ISSN 2076-3921).
Deadline for manuscript submissions: closed (31 October 2020).
Interests: 2-Cys peroxiredoxin; Prx-interacting partners; stress signaling; chaperone activity; post-translational modifications; redox regulation
In 1987, Kim and colleagues identified the first peroxiredoxin (Prx) protein, a thiol-specific antioxidant, in yeast [1,2]. Since then, researchers have identified six isoforms of Prx in mammalian cells alone. Prxs are key molecules in intracellular ROS homeostasis that play important biological roles in various cellular processes including cell growth, differentiation, apoptosis, the immune response, and metabolism. In addition, Prxs have been found to play roles in a variety of post-translational modifications such as phosphorylation, ubiquitination, and glutathionylation.
The goal of this Special Issue is to bring together current views, new insights, and cutting-edge research on the biological roles of Prxs. These include Prxs sourced from all species, from prokaryotes to eukaryotes, including those found in E. coli, plants, yeasts, and animals.
I look forward to your contribution.
- Kim, K., Kim, I.H., Lee, K.Y., Rhee, S.G., and Stadtman, E.R (1988). The isolation and purification of a specific “protector” protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system. J. Biol. Chem. 263, 4704-4711.
- Kim, I.H., Kim, K., and Rhee, S.G (1989). Induction of an antioxidant protein of Saccharomyces cerevisiae by O2, Fe3+, or 2-mercaptoethanol. Proc. Natl. Acad. Sci. USA. 86, 6018-6022.
Prof. Ho Hee Jang
Manuscript Submission Information
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- reactive oxygen species
- stress response
- redox signaling
- peroxidase activity
- chaperone activity
- protein–protein interaction
- post-translational modifications
- Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family in Antioxidants (11 articles)
- The Role of Peroxiredoxins in Cancer in Antioxidants (5 articles)