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Peroxiredoxins are conserved thiol peroxidases for peroxide detoxification, redox signaling, and chaperone activity. Peroxiredoxin 1-type typical 2-Cys peroxiredoxins are present in both prokaryotes and eukaryotes, with multiple closely related isoforms often coexisting within the same subcellular c...
ORGANISM(S): Escherichia coli Saccharomyces cerevisiae (Baker's yeast) 
2026-03-11 | PXD060819 | Pride
Redox signaling is controlled by the reversible oxidation of cysteine thiols, a post-translational modification triggered by H2O2 acting as a second messenger. However, H2O2 reacts poorly with most cysteine thiols and it is not clear how it discriminates between cysteines to trigger appropriate sign...
ORGANISM(S): Homo sapiens (Human) 
2021-05-04 | PXD024114 | Pride
Peroxiredoxins are ubiquitous thiol-dependent peroxidases for which chaperone and signaling roles have been reported in various types of organisms in the last years. In plants, the peroxidase function of the two typical plastidial 2-Cys peroxiredoxins (2-Cys PRX A and B) has been highlighted while t...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2016-10-11 | PXD003923 | Pride
Oxidation of thiol proteins and redox signaling occur in cells exposed to H2O2 but mechanisms are unclear. We used redox proteomics to seek evidence of oxidation of specific proteins either by a mechanism involving reaction of H2O2 with CO2/bicarbonate to give the more reactive peroxymonocarbonate...
ORGANISM(S): Homo Sapiens 
2024-07-08 | PXD053738 |
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