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ProteomicsIdentification of A. thaliana 2-Cys peroxiredoxins interacting proteins
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
A. thaliana Peroxiredoxins Nanolc-ms/ms Interactome 
Genomics2-Cys peroxiredoxins and the chaperone cpHSP70 act in concert in chloroplast biogenesis in Arabidopsis seedlings
2-Cys peroxiredoxins and the chaperone cpHSP70 act in concert in chloroplast biogenesis in Arabidopsis seedlings
PRJNA1201151 | ENA
ProteomicsThe Human 2-Cys Peroxiredoxins Form Widespread, Cysteine-Dependent- And Isoform-Specific Protein-Protein Interactions.
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
Protein thiol oxidation Cysteine sulfenic acid Hydrogen peroxide Thiol disulfide exchange Peroxiredoxin  redox signaling  redox relay 
ProteomicsHeterooligomerisation is a conserved feature of eukaryotic typical 2-Cys peroxiredoxins
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
Heterooligomers Eukaryotes Redox homeostasis Peroxiredoxins 
Transcriptomics2-Cys peroxiredoxins and the chaperone cpHSP70 act in concert in chloroplast biogenesis in Arabidopsis seedlings
The redox balance between NADPH-dependent thioredoxin reductase C (NTRC) and 2-Cys peroxiredoxins (PRXs) help chloroplast photosynthetic performance acclimate rapidly to environmental cues. The Arabidopsis (Arabidopsis thaliana) 2cpab mutant, which lacks chloroplast 2-Cys PRXs A and B, shows impaire...
ORGANISM(S): Arabidopsis thaliana 
2026-04-05 | GSE285083 | GEO
ProteomicsTwo opposing redox signals mediated by 2-Cys peroxiredoxin shape the redox proteome during photosynthetic induction
Photosynthetic induction, characterized by the lag in CO2 assimilation rates during transition from darkness to light, has traditionally been attributed to Rubisco activase activity and stomatal opening. Yet, the faster induction of photosynthesis in the 2-Cys peroxiredoxins (Prxs) mutant (2cpab) su...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-08-25 | PXD065702 | Pride
Photosynthesis induction Redox proteomics Lc-ms Redox signaling Spear 2-cys peroxiredoxins 
UnknownTypical 2-Cys peroxiredoxins--structures, mechanisms and functions.
Not available
S-EPMC2747500 | biostudies-literature
ProteomicsTwo opposing redox signals mediated by 2-Cys peroxiredoxin shape the redox proteome during photosynthetic induction
Photosynthetic induction, characterized by the lag in CO2 assimilation rates during transition from darkness to light, has traditionally been attributed to Rubisco activase activity and stomatal opening. Yet, the faster induction of photosynthesis in the 2-Cys peroxiredoxins (Prxs) mutant (2cpab) su...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-08-25 | PXD065993 | Pride
Arabidopsis Photosynthesis induction Redox proteomics N-ethylmaleimide Redox signaling Nem 2-cys peroxiredoxins 
UnknownHow pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily.
Not available
S-EPMC4375507 | biostudies-literature
UnknownPlastid 2-Cys peroxiredoxins are essential for embryogenesis in Arabidopsis.
Not available
S-EPMC10020101 | biostudies-literature
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