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• W2256070294 abstract "Peroxiredoxins are ubiquitous proteins that are found from bacteria to humans. Until recently they were thought to solely act as antioxidants catalysing the reduction of peroxides through their associated thioredoxin peroxidase activity. However, recent work has begun to uncover hitherto unsuspected roles for one group of these proteins, the typical 2-Cys peroxiredoxins (2-Cys Prx). For example, typical 2-Cys Prxs have been found to have roles in the model organisms Schizosaccharomvces pombe and Saccharomyces cerevisiae in regulating signal transduction, in DNA damage responses and as molecular chaperones. There is increasing evidence that H2O2 is utilised as a signalling molecule to regulate a range of important cellular processes. As abundant and ubiquitous peroxidase enzymes the peroxidase activity of typical 2-Cys Prxs is important in the regulation of these functions. Significantly, studies in yeast suggest that the regulation of the thioredoxin peroxidase and chaperone activities of these multifunction enzymes is an important aspect of H2O2-mediated signal transduction and consequently have provided important insight into the roles of these proteins in higher eukaryotes." @default.
• W2256070294 created "2016-06-24" @default.
• W2256070294 creator A5000244740 @default.
• W2256070294 creator A5064370058 @default.
• W2256070294 date "2007-01-01" @default.
• W2256070294 modified "2023-09-27" @default.
• W2256070294 title "Functions of Typical 2-Cys Peroxiredoxins in Yeast" @default.
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• W2256070294 doi "https://doi.org/10.1007/978-1-4020-6051-9_12" @default.
• W2256070294 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18084898" @default.
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