GO:0051920 peroxiredoxin activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0051920 (peroxiredoxin activity) is a molecular_function defined as catalysis of the reaction [protein]-dithiol + ROOH = [protein]-disulfide + H2O + ROH, using a conserved peroxidatic cysteine to reduce hydroperoxides.
• Peroxiredoxins (PRDXs) are thiol-dependent peroxidases that control hydrogen peroxide and organic hydroperoxide levels, thereby shaping redox signaling and protecting cells from oxidative damage.
• PRDX1, PRDX2, PRDX5 and PRDXQ are experimentally validated members whose peroxidase activity has been linked to inflammation, kidney injury, myocardial ischemia-reperfusion injury, immune modulation and plant lipid desaturation [1,3,4,5,6,7,8].
• Peroxiredoxin activity is not merely antioxidant housekeeping: PRDX1 can inhibit TRAF6 ubiquitin-ligase activity and NFKB activation, while PRDX1 can also aggravate acute kidney injury through Mincle/Syk/NF-κB signaling [3,4].
• Small molecules and metabolites can inhibit peroxiredoxin activity: palmitic acid inhibits PRDX1 peroxidase activity in nonalcoholic steatohepatitis, Epo-C12 inhibits PRDX1 peroxidase activity, and itaconate inhibits PRDX5 [1,5,6].
• CRISPR knockout, point-mutation, knock-in and overexpression models are essential to test whether a candidate peroxiredoxin gene is causally involved in a given redox or disease phenotype.
Description
Peroxiredoxin activity (GO:0051920) is a molecular_function that describes the catalytic reduction of hydroperoxides by thiol-containing peroxiredoxin enzymes. The reaction converts a protein dithiol and a hydroperoxide (ROOH) into a protein disulfide, water and the corresponding alcohol (ROH), placing peroxiredoxins among the primary enzymatic defenses against reactive oxygen species and a key node in redox signaling. Because hydrogen peroxide and organic hydroperoxides act as second messengers, the activity of peroxiredoxins directly influences how cells interpret oxidative cues. Researchers study GO:0051920 to understand how cells balance oxidative stress, inflammation and survival, and to identify therapeutic opportunities in metabolic, renal, cardiovascular and immune disorders [1,3,6,7]. The family includes multiple isoforms with distinct tissue distributions and subcellular localizations, and their catalytic cycles depend on a conserved peroxidatic cysteine that is oxidized to sulfenic acid and then resolved through disulfide formation. Beyond canonical antioxidant chemistry, peroxiredoxin activity can modulate signaling complexes: PRDX1 inhibits TRAF6 ubiquitin-ligase activity and NFKB activation, illustrating how a peroxidase can directly shape innate immune signaling. Conversely, PRDX1 can promote inflammation through Mincle/Syk/NF-κB signaling in acute kidney injury, showing that the biological outcome of peroxiredoxin activity is context-dependent. This article integrates the QuickGO definition with verified experimental literature to summarize the mechanism, key genes, disease links and CRISPR-based research strategies for GO:0051920.
peroxiredoxin activity At A Glance
| GO ID | GO:0051920 |
|---|---|
| GO term | peroxiredoxin activity |
| Ontology | molecular_function |
| Synonym | PRDX activity; Prx activity |
| Definition | Catalysis of the reaction: [protein]-dithiol + ROOH = [protein]-disulfide + H2O + ROH |
| Major function | Thiol-dependent reduction of hydrogen peroxide and organic hydroperoxides, contributing to redox homeostasis and redox signaling |
| Representative enzymes | PRDX1, PRDX2, PRDX5, PRDXQ and other peroxiredoxin family members [1,3,4,5,6,7,8] |
| Catalytic feature | Conserved peroxidatic cysteine oxidized to sulfenic acid and resolved via disulfide formation |
| Disease relevance | Nonalcoholic steatohepatitis, acute kidney injury, myocardial ischemia-reperfusion injury, immune modulation [1,3,6,7] |
What Is GO:0051920?
In practical terms, GO:0051920 describes the enzymatic activity of a peroxiredoxin: a thiol peroxidase that uses a redox-active cysteine to reduce a hydroperoxide substrate. The formal QuickGO definition is catalysis of the reaction [protein]-dithiol + ROOH = [protein]-disulfide + H2O + ROH. This means the enzyme transfers reducing equivalents from its own cysteine thiols to the peroxide, producing water and an alcohol while the protein itself becomes oxidized to a disulfide. The activity is therefore both a detoxification reaction and a redox relay, because the oxidized peroxiredoxin must subsequently be reduced by cellular thiol systems to complete a catalytic cycle. Synonyms include PRDX activity and Prx activity.
Why Is peroxiredoxin activity Important in Cell Biology?
Peroxiredoxin activity is important because it sits at the intersection of antioxidant defense and signal transduction. By controlling the steady-state concentration of hydrogen peroxide and organic hydroperoxides, peroxiredoxins influence whether oxidative signals are propagated or terminated, which affects cell proliferation, inflammation, autophagy and survival [2,4]. Experimental studies show that perturbing this activity has direct pathophysiological consequences: inhibition of PRDX1 peroxidase activity by palmitic acid exacerbates nonalcoholic steatohepatitis in male mice, PRDX1 aggravates acute kidney injury by promoting inflammation through Mincle/Syk/NF-κB signaling, and PRDX2 alleviates myocardial ischemia-reperfusion injury by inhibiting platelet activity via the AKT/NF-κB pathway. In addition, PRDX1 can inhibit TRAF6 ubiquitin-ligase activity and NFKB activation, linking peroxidase chemistry to autophagy regulation. These findings make GO:0051920 a high-value target for mechanistic studies and for therapeutic strategies aimed at modulating redox signaling in metabolic, renal, cardiovascular and immune diseases.
• Controls hydrogen peroxide and organic hydroperoxide levels, thereby shaping redox signaling and oxidative stress responses.
• Protects cells from oxidative damage through thiol-dependent peroxidase chemistry.
• Modulates innate immune and inflammatory signaling, including NFKB and Mincle/Syk/NF-κB pathways [3,4].
• Is implicated in metabolic liver disease: palmitic acid inhibition of PRDX1 peroxidase activity exacerbates nonalcoholic steatohepatitis in male mice.
• Is implicated in acute kidney injury through PRDX1-driven inflammation.
• Is implicated in myocardial ischemia-reperfusion injury through PRDX2 and platelet activity.
• Can be targeted pharmacologically, as shown by Epo-C12 inhibition of PRDX1 peroxidase activity.
• Can be modulated by endogenous metabolites, as shown by itaconate inhibition of PRDX5.
• Has non-mammalian roles, including stimulation of chloroplast fatty acid desaturase activity by PEROXIREDOXIN Q.
• Provides a tractable enzymatic activity for CRISPR-based causal testing of redox genes in disease models.
Molecular Mechanism of peroxiredoxin activity
Peroxidatic cysteine oxidation
In simple terms: The enzyme uses a special cysteine to grab oxygen from the peroxide.
The catalytic cycle of peroxiredoxin activity begins when a conserved peroxidatic cysteine attacks the hydroperoxide substrate (ROOH). This step reduces the peroxide to water and the corresponding alcohol (ROH) while the cysteine is oxidized to a sulfenic acid intermediate. The overall reaction is [protein]-dithiol + ROOH = [protein]-disulfide + H2O + ROH, as defined for GO:0051920. This chemistry is the foundation of thiol-dependent peroxide detoxification and redox signaling control.
Disulfide formation and resolution
In simple terms: After grabbing the oxygen, the enzyme forms a disulfide bond that must be undone to reset the enzyme.
Following oxidation of the peroxidatic cysteine, the enzyme resolves the sulfenic acid by forming a disulfide bond, either with a resolving cysteine within the same protein or with another thiol. This converts the protein to its disulfide state, consistent with the product side of the GO:0051920 reaction. The disulfide must then be reduced by cellular thiol systems to regenerate the active dithiol form and complete the catalytic cycle.
Redox relay and signaling modulation
In simple terms: Peroxiredoxins do not just remove peroxide; they can pass the oxidative signal to other proteins.
Peroxiredoxin activity can act as a redox relay, transferring oxidizing equivalents to downstream effectors and thereby modulating signaling. For example, PRDX1 inhibits TRAF6 ubiquitin-ligase activity, leading to inhibition of NFKB activation and activation of autophagy. In acute kidney injury, PRDX1 promotes inflammation through Mincle/Syk/NF-κB signaling, demonstrating that the same activity can drive pathogenic signaling in a specific context. These examples show that GO:0051920 is mechanistically coupled to immune and stress-response pathways.
Substrate specificity and inhibition
In simple terms: Different peroxiredoxins prefer different peroxides, and their activity can be blocked by small molecules.
Peroxiredoxins can reduce hydrogen peroxide and organic hydroperoxides, and their activity can be inhibited by endogenous and synthetic molecules. Palmitic acid inhibits PRDX1 peroxidase activity and exacerbates nonalcoholic steatohepatitis in male mice. Epo-C12 inhibits PRDX1 peroxidase activity, and itaconate modulates immune responses via inhibition of PRDX5. These findings establish that GO:0051920 is a druggable and metabolite-sensitive activity.
Non-mammalian and organellar functions
In simple terms: Peroxiredoxin activity also matters outside animals, including in plant chloroplasts.
In plants, PEROXIREDOXIN Q stimulates the activity of the chloroplast 16:1(Δ3trans) FATTY ACID DESATURASE4, linking peroxiredoxin activity to lipid metabolism in photosynthetic organelles. This conservation underscores that GO:0051920 is not restricted to mammalian antioxidant defense but participates in diverse metabolic processes.
Key Genes Involved in GO:0051920 peroxiredoxin activity
The following genes and proteins are experimentally linked to peroxiredoxin activity (GO:0051920) in the verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| PRDX1 | Thiol-dependent peroxidase; inhibits TRAF6 ubiquitin-ligase activity and NFKB activation; promotes Mincle/Syk/NF-κB inflammation | Studied in nonalcoholic steatohepatitis, acute kidney injury and autophagy regulation [1,3,4] |
| PRDX2 | Peroxiredoxin that inhibits platelet activity via AKT/NF-κB | Studied in myocardial ischemia-reperfusion injury |
| PRDX5 | Peroxiredoxin targeted by itaconate to modulate immune responses | Studied in immune modulation |
| PRDXQ | Plant peroxiredoxin that stimulates chloroplast fatty acid desaturase activity | Studied in chloroplast lipid metabolism |
| TRAF6 | Ubiquitin-ligase inhibited by PRDX1 | Studied in NFKB activation and autophagy |
| NFKB | Transcription factor regulated downstream of peroxiredoxin activity | Studied in inflammation and immune signaling [3,4] |
| Mincle | Innate immune receptor upstream of Syk/NF-κB in PRDX1-driven inflammation | Studied in acute kidney injury |
| Syk | Kinase in the Mincle/Syk/NF-κB pathway | Studied in PRDX1-mediated inflammation |
| AKT | Kinase pathway affected by PRDX2 in platelets | Studied in myocardial ischemia-reperfusion injury |
| FATTY ACID DESATURASE4 | Chloroplast desaturase stimulated by PEROXIREDOXIN Q | Studied in plant lipid metabolism |
| Palmitic acid | Endogenous fatty acid that inhibits PRDX1 peroxidase activity | Studied in nonalcoholic steatohepatitis |
| Epo-C12 | Small-molecule inhibitor of PRDX1 peroxidase activity | Studied as a chemical probe |
| Itaconate | Metabolite that inhibits PRDX5 | Studied in immune modulation |
| Hydrogen peroxide | Substrate of peroxiredoxin activity | Studied in redox signaling |
| Organic hydroperoxides | Substrates of peroxiredoxin activity | Studied in oxidative stress and signaling |
| Peroxidatic cysteine | Catalytic residue oxidized during the reaction | Studied in enzyme mechanism |
| Resolving cysteine | Residue that resolves the sulfenic acid to a disulfide | Studied in catalytic cycle |
| Thiol reductants | Cellular systems that regenerate reduced peroxiredoxin | Studied in catalytic cycle |
How Is peroxiredoxin activity Regulated?
Peroxiredoxin activity is regulated at multiple levels. Catalytically, the enzyme cycles between reduced dithiol and oxidized disulfide states, and its activity depends on the availability of reducing equivalents to resolve the disulfide and regenerate the active form. Post-translational modifications and interacting partners can influence this cycle, as illustrated by PRDX1 inhibition of TRAF6 ubiquitin-ligase activity, which couples peroxidase function to NFKB and autophagy regulation. Endogenous metabolites and lipids can also regulate activity: palmitic acid inhibits PRDX1 peroxidase activity and exacerbates nonalcoholic steatohepatitis in male mice, and itaconate inhibits PRDX5 to modulate immune responses. Pharmacological inhibitors such as Epo-C12 can block PRDX1 peroxidase activity, providing chemical tools to probe regulation. In plants, PEROXIREDOXIN Q stimulates chloroplast fatty acid desaturase activity, indicating that regulation extends to organellar lipid metabolism.
peroxiredoxin activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PRDX1 | Nonalcoholic steatohepatitis; acute kidney injury; autophagy and NFKB regulation | PRDX1 knockout or point-mutant hepatocytes and kidney cells; palmitic acid treatment [1,3,4] |
| PRDX2 | Myocardial ischemia-reperfusion injury; platelet activity | PRDX2 knockout or overexpression in cardiomyocytes and platelets |
| PRDX5 | Immune modulation | PRDX5 knockout macrophages treated with itaconate |
| PRDXQ | Chloroplast lipid metabolism | Plant PRDXQ knockout or overexpression lines |
| TRAF6 | NFKB activation and autophagy | TRAF6 knockout or knock-in cells with PRDX1 perturbation |
Nonalcoholic steatohepatitis
Inhibited peroxidase activity of PRDX1 by palmitic acid exacerbates nonalcoholic steatohepatitis in male mice, linking GO:0051920 directly to metabolic liver disease. This suggests that preserving or restoring PRDX1 peroxidase activity could be a therapeutic strategy in steatohepatitis.
Acute kidney injury
PRDX1 aggravates acute kidney injury by promoting inflammation through Mincle/Syk/NF-κB signaling, demonstrating that peroxiredoxin activity can drive pathogenic inflammation in the kidney. This creates a rationale for targeting PRDX1-dependent signaling in renal injury.
Myocardial ischemia-reperfusion injury
PRDX2 alleviates myocardial ischemia-reperfusion injury by inhibiting platelet activity via the AKT/NF-κB pathway, indicating a protective role for this peroxiredoxin in cardiovascular injury.
Immune modulation and inflammation
Itaconate modulates immune responses via inhibition of PRDX5, and PRDX1 inhibits TRAF6 ubiquitin-ligase activity to inhibit NFKB activation and activate autophagy [4,6]. These findings position peroxiredoxin activity as a node in innate immune and inflammatory regulation.
From peroxiredoxin activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of PRDX1 peroxidase activity alter steatohepatitis progression? | PRDX1 knockout or catalytically dead point-mutant hepatocytes and mouse models |
| Does PRDX1 drive acute kidney injury through Mincle/Syk/NF-κB? | PRDX1 knockout kidney cells and pathway inhibitors |
| Does PRDX1 inhibit TRAF6 ubiquitin-ligase activity? | PRDX1 knockout or overexpression with TRAF6 signaling readouts |
| Can small molecules inhibit PRDX1 peroxidase activity? | PRDX1 overexpression cells treated with Epo-C12 |
| Does itaconate modulate immunity through PRDX5 inhibition? | PRDX5 knockout macrophages treated with itaconate |
| Does PRDX2 protect against myocardial ischemia-reperfusion injury? | PRDX2 knockout or overexpression in cardiomyocytes and platelets |
How to Study the peroxiredoxin activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Peroxidase activity assay | Reduction of hydroperoxide substrates | Testing PRDX1 inhibition by palmitic acid or Epo-C12 [1,5] |
| Western blot for pathway proteins | NFKB, AKT and related signaling changes | Linking peroxiredoxin activity to inflammation and survival [3,4,7] |
| CRISPR knockout | Loss-of-function phenotype | Testing causal role of PRDX1, PRDX2 or PRDX5 [1,3,7] |
| CRISPR point mutation | Catalytic cysteine function | Separating peroxidase activity from scaffolding functions |
| Overexpression | Gain-of-function phenotype | Testing protective or pathogenic effects of peroxiredoxins [4,7] |
| Metabolite profiling | Itaconate and lipid levels | Understanding endogenous regulation of peroxiredoxin activity [1,6] |
| Plant genetic models | Chloroplast lipid desaturation | Studying PRDXQ in plant metabolism |
Enzymatic activity assays
Peroxiredoxin activity can be measured by monitoring the reduction of hydroperoxide substrates, such as hydrogen peroxide or organic hydroperoxides, in the presence of thiol reductants. These assays are used to test inhibitors such as palmitic acid and Epo-C12, and to compare wild-type and mutant enzymes [1,5].
Redox and signaling readouts
Because peroxiredoxin activity controls redox signaling, researchers measure downstream pathways such as NFKB, Mincle/Syk/NF-κB and AKT/NF-κB to link enzymatic activity to cellular outcomes [3,4,7].
Genetic perturbation with CRISPR
CRISPR knockout, point mutation, knock-in and overexpression models allow causal testing of peroxiredoxin genes in disease phenotypes, including steatohepatitis, kidney injury and myocardial ischemia-reperfusion injury [1,3,7].
Metabolite and inhibitor profiling
Endogenous metabolites such as itaconate and lipids such as palmitic acid can regulate peroxiredoxin activity, so metabolite profiling and inhibitor studies are used to define the regulatory landscape of GO:0051920 [1,6].
How CRISPR Can Be Used to Study GO:0051920 peroxiredoxin activity
Knockout
CRISPR knockout of PRDX1, PRDX2 or PRDX5 can remove peroxiredoxin activity and reveal its contribution to disease phenotypes such as steatohepatitis, acute kidney injury and myocardial ischemia-reperfusion injury [1,3,7]. Knockout models are also useful to test whether a phenotype depends on the peroxidase activity or on other functions of the protein.
Point Mutation
Point mutation of the peroxidatic cysteine can abolish catalytic activity while preserving protein structure, allowing researchers to separate the enzymatic function of GO:0051920 from non-catalytic roles. This is particularly relevant for PRDX1, which has both peroxidase and signaling functions [2,4].
Knock-in
Knock-in of tagged or mutant peroxiredoxin alleles enables tracking of protein localization, interaction partners and redox state in cells and tissues. Such models can be combined with disease challenges to map where peroxiredoxin activity matters [2,3].
Overexpression
Overexpression of PRDX1, PRDX2 or PRDX5 can test gain-of-function effects, including protection against oxidative injury or exacerbation of inflammation. Overexpression systems are also used to evaluate inhibitors such as Epo-C12 and itaconate [4,5,6,7].
How EDITGENE Supports peroxiredoxin activity Research
Researchers studying peroxiredoxin activity-related genes often need to determine whether a candidate gene is causally involved in a redox or disease phenotype, and CRISPR-based models provide the most direct way to test this. EDITGENE supports these studies with knockout, point-mutation, knock-in, overexpression cell models and CRISPR library screening / bioinformatics services.
Contact EDITGENE today to design your custom CRISPR model for peroxiredoxin activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| PRDX6 Knockout SRA01/04 Cell Line | EDJ-KQ67 | Human | 9588 | Details Get a Quote |
| Park7 Knockout HT22 Cell Line | EDJ-KQ72 | Mouse | 57320 | Details Get a Quote |
| Prdx6 Knockout TM4 Cell Line | EDJ-KQ76 | Mouse | 11758 | Details Get a Quote |
| PARK7 Knockout HEK293 Cell Line | EDJ-KQ969 | Human | 11315 | Details Get a Quote |
| PRDX6 Knockout HEK293 Cell Line | EDJ-KQ1098 | Human | 9588 | Details Get a Quote |
| PRDX4 Knockout HEK293 Cell Line | EDJ-KQ3662 | Human | 10549 | Details Get a Quote |
| PRDX1 Knockout HEK293 Cell Line | EDJ-KQ3965 | Human | 5052 | Details Get a Quote |
| PRDX3 Knockout HEK293 Cell Line | EDJ-KQ7218 | Human | 10935 | Details Get a Quote |
| PRDX2 Knockout HEK293 Cell Line | EDJ-KQ11963 | Human | 7001 | Details Get a Quote |
| PARK7 Knockout A-549 Cell Line | EDJ-KQ19975 | Human | 11315 | Details Get a Quote |
| PARK7 Knockout HeLa Cell Line | EDJ-KQ19977 | Human | 11315 | Details Get a Quote |
| PRDX3 Knockout A-549 Cell Line | EDJ-KQ32173 | Human | 10935 | Details Get a Quote |
| PRDX3 Knockout HCT 116 Cell Line | EDJ-KQ32174 | Human | 10935 | Details Get a Quote |
| PRDX3 Knockout HeLa Cell Line | EDJ-KQ32175 | Human | 10935 | Details Get a Quote |
| PARK7 Knockout HCT 116 Cell Line | EDJ-KQ18655 | Human | 11315 | Details Get a Quote |
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Frequently Asked Questions About peroxiredoxin activity
What is peroxiredoxin activity?
Peroxiredoxin activity (GO:0051920) is a molecular_function defined as catalysis of the reaction [protein]-dithiol + ROOH = [protein]-disulfide + H2O + ROH, using a conserved cysteine to reduce hydroperoxides.
What genes are involved in peroxiredoxin activity?
Key genes include PRDX1, PRDX2, PRDX5 and PRDXQ, which encode peroxiredoxin enzymes with experimentally characterized roles in redox signaling and disease [1,3,4,5,6,7,8].
What is the GO ID for peroxiredoxin activity?
The GO ID for peroxiredoxin activity is GO:0051920.
How does peroxiredoxin activity work?
A peroxidatic cysteine attacks a hydroperoxide, forming a sulfenic acid that resolves into a disulfide; the enzyme is then reduced to complete the cycle.
What diseases are linked to peroxiredoxin activity?
Peroxiredoxin activity has been linked to nonalcoholic steatohepatitis, acute kidney injury, myocardial ischemia-reperfusion injury and immune modulation [1,3,6,7].
Can peroxiredoxin activity be inhibited?
Yes, palmitic acid inhibits PRDX1 peroxidase activity, Epo-C12 inhibits PRDX1 peroxidase activity, and itaconate inhibits PRDX5 [1,5,6].
What is the role of PRDX1 in inflammation?
PRDX1 can inhibit TRAF6 ubiquitin-ligase activity and NFKB activation, but it can also promote inflammation through Mincle/Syk/NF-κB signaling in acute kidney injury [3,4].
How is PRDX2 involved in heart injury?
PRDX2 alleviates myocardial ischemia-reperfusion injury by inhibiting platelet activity via the AKT/NF-κB pathway.
What model systems are used to study peroxiredoxin activity?
CRISPR knockout, point-mutation, knock-in and overexpression cell models, as well as plant genetic models for PRDXQ, are used to study peroxiredoxin activity [1,3,5,7,8].
Why is peroxiredoxin activity important for redox signaling?
By controlling hydrogen peroxide and organic hydroperoxide levels, peroxiredoxins influence whether oxidative signals are propagated or terminated, affecting inflammation, autophagy and survival [2,4].
Conclusion
Peroxiredoxin activity (GO:0051920) is a central thiol-dependent peroxidase activity that reduces hydrogen peroxide and organic hydroperoxides while shaping redox signaling and inflammation. Verified studies link PRDX1, PRDX2, PRDX5 and PRDXQ to metabolic liver disease, acute kidney injury, myocardial ischemia-reperfusion injury, immune modulation and plant lipid metabolism [1,3,4,5,6,7,8]. Because the activity is druggable and metabolite-sensitive, it represents a promising target for mechanistic and therapeutic research. CRISPR-based knockout, point-mutation, knock-in and overexpression models provide the causal evidence needed to translate peroxiredoxin biology into clinical insight.
References
- 1. Yin W et al.. 2025. Inhibited peroxidase activity of peroxiredoxin 1 by palmitic acid exacerbates nonalcoholic steatohepatitis in male mice.. Nat Commun 16(1):598 PMID: 39799115
- 2. Averill-Bates D. 2024. Reactive oxygen species and cell signaling. Review.. Biochim Biophys Acta Mol Cell Res 1871(2):119573 PMID: 37949302
- 3. Li S et al.. 2023. Peroxiredoxin 1 aggravates acute kidney injury by promoting inflammation through Mincle/Syk/NF-κB signaling.. Kidney Int 104(2):305-323 PMID: 37164261
- 4. Min Y et al.. 2018. Inhibition of TRAF6 ubiquitin-ligase activity by PRDX1 leads to inhibition of NFKB activation and autophagy activation.. Autophagy 14(8):1347-1358 PMID: 29929436
- 5. Yoda T et al.. 2021. Epo-C12 inhibits peroxiredoxin 1 peroxidase activity.. Bioorg Med Chem 41:116203 PMID: 34015702
- 6. Paulenda T et al.. 2025. Itaconate modulates immune responses via inhibition of peroxiredoxin 5.. Nat Metab 7(6):1183-1203 PMID: 40251412
- 7. Gu C et al.. 2025. Peroxiredoxin 2 alleviates myocardial ischemia-reperfusion injury by inhibiting platelet activity via the AKT/NF-κB pathway.. Eur J Pharmacol 1002:177855 PMID: 40543739
- 8. Horn PJ et al.. 2020. PEROXIREDOXIN Q stimulates the activity of the chloroplast 16:1(Δ3trans) FATTY ACID DESATURASE4.. Plant J 102(4):718-729 PMID: 31856363
