PRDX2 — Peroxiredoxin 2
Introduction
Prdx2 — Peroxiredoxin 2 is a critical antioxidant enzyme in the neurobiology of neurodegenerative diseases. This page provides comprehensive information about its structure, function, and role in disease processes including Parkinson's disease, Alzheimer's disease, and amyotrophic lateral sclerosis.
<table class="infobox infobox-gene"> [@tasset2012]
<tr> [@klammer2020]
<th class="infobox-header" colspan="2">PRDX2 — Peroxiredoxin 2</th>
</tr>
<tr>
<td class="label">Symbol</td>
<td><strong>PRDX2</strong></td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Peroxiredoxin 2</td>
</tr>
<tr>
<td class="label">Chromosome</td>
<td>19p13.13</td>
</tr>
<tr>
<td class="label">NCBI Gene</td>
<td><a href="https://www.ncbi.nlm.nih.gov/gene/7003" target="_blank">7003</a></td>
</tr>
<tr>
<td class="label">Ensembl</td>
<td><a href="https://ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000167612" target="_blank">ENSG00000167612</a></td>
</tr>
<tr>
<td class="label">OMIM</td>
<td><a href="https://omim.org/entry/607386" target="_blank">607386</a></td>
</tr>
<tr>
<td class="label">UniProt</td>
<td><a href="https://www.uniprot.org/uniprot/P32189" target="_blank">P32189</a></td>
</tr>
<tr>
<td class="label">Diseases</td>
<td>Parkinson's Disease, Alzheimer's Disease, ALS, Stroke</td>
</tr>
<tr>
<td class="label">Expression</td>
<td>Erythrocytes, Brain, Liver, Kidney, Heart</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td><a href="/wiki/als" style="color:#ef9a9a">Als</a>, <a href="/wiki/ms" style="color:#ef9a9a">Ms</a></td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">11 edges</a></td>
</tr>
</table>
Overview
PRDX2 (Peroxiredoxin 2) is a gene located on chromosome 19p13.13 that encodes a member of the peroxiredoxin family of antioxidant proteins. PRDX2 is a typical 2-Cys peroxiredoxin that reduces hydrogen peroxide (H₂O₂), peroxynitrite (ONOO⁻), and organic hydroperoxides, playing crucial roles in cellular antioxidant defense and redox signaling. [@lee2011]
The peroxiredoxin family comprises six isoforms in mammals (PRDX1-6), with PRDX2 being one of the most abundant cytosolic antioxidants. It is particularly highly expressed in erythrocytes and various tissues including brain, liver, kidney, and heart. [@kim2008] PRDX2 functions as both a peroxidase and a molecular chaperone, making it uniquely positioned to protect cells against oxidative damage. [@risoa2009]
Structure and Biochemistry
Molecular Architecture
PRDX2 is a 22-kDa protein composed of 198 amino acids. Its structure consists of:
- N-terminal region: Contains the first conserved cysteine (Cys⁵¹)
- C-terminal region: Contains the resolving cysteine (Cys¹⁷²)
- β-sheet core: Forms the catalytic center
- C-terminal tail: Regulates enzyme activity
The protein exists primarily as a homodimer, with each monomer containing two conserved cysteine residues essential for catalytic activity. The active site contains a "peroxiredoxin signature" motif (FTFVCPTEI) that defines the 2-Cys peroxiredoxin family. [@wang2014]
Catalytic Mechanism
The enzymatic cycle of PRDX2 involves:
Peroxidation: The active-site peroxidatic cysteine (Cys⁵¹) reacts with H₂O₂ to form a sulfenic acid (SOH)
Disulfide formation: The sulfenic acid condenses with the resolving cysteine (Cys¹⁷²) to form an intramolecular disulfide
Reduction: Thioredoxin (Trx) or thioredoxin reductase reduces the disulfide back to the active dithiol form
Regeneration: The reduced enzyme is ready for another catalytic cycleThis catalytic mechanism allows PRDX2 to detoxify H₂O₂ at rates approaching diffusion-limited reactions, making it one of the most efficient antioxidant enzymes in the cell. [@yang2009]
Oligomerization and Chaperone Activity
Under oxidative stress conditions, PRDX2 undergoes a structural transition from a dimeric peroxidase to a high-molecular-weight decameric complex. This oligomerization is induced by:
- Hyperoxidation of the active-site cysteine (Cys-SOH)
- Phosphorylation at specific residues
- Oxidative modifications
The decameric form exhibits chaperone activity, protecting proteins from oxidative aggregation. This dual functionality—peroxidase and chaperone—makes PRDX2 particularly important in neurodegenerative conditions where protein aggregation is a hallmark. [@hu2009]
Function
Antioxidant Defense
PRDX2 is a central component of the cellular antioxidant defense system:
- Hydrogen peroxide detoxification: Reduces H₂O₂ to water using thioredoxin as the electron donor
- Peroxynitrite scavenging: Protects against peroxynitrite (ONOO⁻), a highly reactive nitrogen species
- Organic hydroperoxide reduction: Reduces lipid hydroperoxides, protecting membrane integrity
- Redox signaling modulation: Controls the levels of H₂O₂ that serve as second messengers
In neurons, PRDX2 provides critical protection against oxidative damage from multiple sources including mitochondrial electron transport leak, inflammatory responses, and environmental toxins. [@mann2006]
Molecular Chaperone Function
When oxidized beyond its peroxidase capacity, PRDX2 transitions to a chaperone form that:
- Prevents protein aggregation under oxidative stress
- Helps refold denatured proteins
- Protects against heat-induced protein damage
- Maintains cellular proteostasis
This chaperone function is particularly important in [neurons](/entities/neurons), which are post-mitotic and cannot dilute damaged proteins through cell division. [@fujii2010]
Regulation of Cell Death Pathways
PRDX2 interacts with multiple cell death pathways:
- Inhibition of apoptosis: By reducing oxidative stress and maintaining mitochondrial integrity
- Regulation of JNK signaling: Oxidized PRDX2 releases ASK1, affecting downstream pro-apoptotic signals
- Protection against necroptosis: By scavenging ROS that trigger necrotic cell death pathways
The balance between PRDX2's peroxidase and pro-apoptotic functions is regulated by its oxidation state and oligomeric status. [@yang2007]
Expression and Localization
Tissue Distribution
PRDX2 shows widespread expression:
- Erythrocytes: Highest expression (~50% of cytosolic protein)
- Brain: Neuronal expression in cortex, hippocampus, cerebellum
- Liver: Hepatocyte expression
- Kidney: Renal tubular cells
- Heart: Cardiomyocytes
In the brain, PRDX2 is expressed in both neurons and glia, with particular enrichment in [dopaminergic neurons](/cell-types/dopaminergic-neurons) of the substantia nigra—neurons that degenerate in Parkinson's disease. [@eng2015]
Subcellular Localization
- Cytosol: Primary location (~90% of cellular PRDX2)
- Mitochondria: A fraction localizes to mitochondria
- Nucleus: Some nuclear localization reported
- Membrane: Association with plasma membrane under certain conditions
The cytosolic pool provides general antioxidant protection, while the mitochondrial fraction specifically protects against oxidative damage from electron transport chain leakage. [@ng2016]
Disease Associations
Parkinson's Disease
PRDX2 is oxidized and functionally inactivated in [Parkinson's disease](/diseases/parkinsons-disease) brain. Studies show:
- Increased oxidation: PRDX2 shows higher levels of sulfinic/sulfonic acid oxidation in PD substantia nigra
- Decreased activity: Enzymatic activity is reduced by ~40% in PD brain compared to controls
- Interaction with alpha-synuclein: PRDX2 colocalizes with [alpha-synuclein](/proteins/alpha-synuclein) aggregates in Lewy bodies
- Neuroprotection: Overexpression of PRDX2 protects dopaminergic neurons in models of PD
The oxidation of PRDX2 in PD may be both a consequence of increased oxidative stress and a contributor to disease progression through loss of antioxidant and chaperone functions. [@perez2018]
Key mechanisms in PD:
Mitochondrial complex I deficiency leads to increased ROS production
PRDX2 is overwhelmed and becomes hyperoxidized
Loss of peroxidase activity leads to further oxidative damage
Loss of chaperone activity contributes to alpha-synuclein aggregation
Creates a vicious cycle of oxidative damage and protein aggregationAlzheimer's Disease
In [Alzheimer's disease](/diseases/alzheimers-disease), PRDX2 shows altered expression and oxidation:
- Altered levels: PRDX2 expression is changed in AD brain regions vulnerable to pathology
- Oxidation: Hyperoxidized PRDX2 is found in AD hippocampus and cortex
- Amyloid-beta interaction: PRDX2 may protect against [amyloid-beta](/proteins/amyloid-beta) toxicity
- Tau pathology: PRDX2 oxidation correlates with tau pathology severity
PRDX2 may protect against amyloid-beta-induced oxidative damage, and its downregulation in AD may contribute to the oxidative stress that drives disease progression. [@kim2019]
Amyotrophic Lateral Sclerosis (ALS)
PRDX2 oxidation has been reported in ALS models and patients:
- Motor neuron vulnerability: Motor neurons show reduced PRDX2 compared to other neuronal populations
- SOD1 interaction: PRDX2 may interact with mutant SOD1, which causes familial ALS
- Oxidative stress: PRDX2 oxidation in ALS motor cortex correlates with disease duration
The selective vulnerability of motor neurons in ALS may be related to their relatively low PRDX2 levels compared to other neuronal populations. [@yang2020]
Stroke and Ischemic Injury
PRDX2 provides neuroprotection against ischemic injury:
- Preconditioning: PRDX2 overexpression protects against cerebral ischemia
- Reperfusion injury: PRDX2 levels decrease during reperfusion, contributing to oxidative damage
- Therapeutic potential: PRDX2-based therapies are being explored for stroke treatment
- Post-stroke recovery: PRDX2 affects rehabilitation outcomes through oxidative stress modulation
In models of focal cerebral ischemia, PRDX2 overexpression reduces infarct size and improves functional outcomes. Studies have shown that PRDX2 administration either as protein therapy or through gene delivery can significantly reduce brain damage following stroke. [@chen2019]
Multiple System Atrophy (MSA)
PRDX2 alterations have been observed in MSA:
- Oligodendrocyte vulnerability: Reduced PRDX2 in oligodendrocytes
- Myelin dysfunction: Connections to white matter pathology
- Autonomic dysfunction: PRDX2 in autonomic nuclei
- Progression markers: Correlation with disease severity
Progressive Supranuclear Palsy (PSP)
PRDX2 is implicated in PSP pathophysiology:
- Brainstem vulnerability: PRDX2 changes in midbrain structures
- Tau pathology intersection: Overlap with tauopathies
- Neurodegeneration pattern: Region-specific alterations
- Biomarker potential: CSF PRDX2 as PSP marker
Frontotemporal Dementia (FTD)
In FTD, PRDX2 shows:
- Frontal cortex involvement: Altered expression in affected regions
- TDP-43 pathology: Interaction with protein aggregates
- Behavioral variant correlations: Links to behavioral changes
- Language variant associations: Specific patterns in primary progressive aphasia
Other Neurodegenerative Conditions
- Huntington's disease: PRDX2 oxidation in striatum
- Multiple sclerosis: PRDX2 as a biomarker for disease activity
- Friedreich's ataxia: PRDX2 dysfunction due to frataxin deficiency
- Multiple System Atrophy: PRDX2 alterations in oligodendrocytes
- Progressive Supranuclear Palsy: PRDX2 in tau pathology regions
- Frontotemporal Dementia: PRDX2 in frontal and temporal cortex
Ferroptosis and PRDX2
Iron-Dependent Cell Death
Ferroptosis is a recently characterized form of regulated cell death that is distinct from apoptosis and necrosis. It is driven by iron-dependent lipid peroxidation, and PRDX2 plays a critical role in regulating this process in neurons[@nagai2019].
Mechanisms of PRDX2 protection against ferroptosis:
- Scavenging lipid hydroperoxides before they accumulate to lethal levels
- Protecting cell membranes from iron-catalyzed oxidative damage
- Maintaining the balance between pro-oxidant and antioxidant systems
Relevance to neurodegeneration:
- Ferroptosis has been implicated in Parkinson's disease dopaminergic neuron loss
- Iron accumulation in the substantia nigra is a hallmark of PD
- PRDX2 dysfunction may sensitize neurons to ferroptotic cell death
The intersection of iron metabolism and redox homeostasis makes PRDX2 particularly important:
- Iron catalyzes the Fenton reaction, generating hydroxyl radicals
- PRDX2 directly reduces lipid peroxides before they react with iron
- The thioredoxin-PRDX2 system provides the reducing equivalents needed for this protection
Neuroinflammation and PRDX2
Glial Cell Interactions
PRDX2 is not only important in neurons but also regulates inflammatory responses in glial cells[@kar2018]:
Microglial Function:
- PRDX2 modulates microglial activation states
- Loss of PRDX2 promotes pro-inflammatory (M1) phenotype
- PRDX2 overexpression reduces neurotoxic cytokine release
Astrocyte Support:
- Astrocytic PRDX2 supports neuronal antioxidant defense
- Glial PRDX2 contributes to the antioxidant shield of the neuropil
- Cross-talk between neuronal and glial PRDX2 systems
Inflammatory Signaling Modulation
PRDX2 affects multiple inflammatory pathways:
- NF-κB signaling is regulated by the redox state
- MAPK pathways are modulated by PRDX2 activity
- Inflammasome activation is influenced by cellular peroxide levels
Post-Translational Modifications
Redox-Sensitive Regulation
PRDX2 function is highly regulated by post-translational modifications that sense the cellular redox state[@thomson2015]:
Sulfenylation (SOH):
- The peroxidatic cysteine can be oxidized to sulfenic acid
- This is the first step in the catalytic cycle
- Excessive sulfenylation can lead to inactivation
Sulfination (SO₂H) and Sulfonation (SO₃H):
- Hyperoxidation to sulfinic and sulfonic acid forms is largely irreversible
- These forms cannot be reduced by the thioredoxin system
- Accumulation of hyperoxidized PRDX2 is a marker of oxidative stress
S-Nitrosylation:
- NO can modify cysteine residues
- S-nitrosylation can inhibit PRDX2 activity
- This connects nitrative stress to antioxidant dysfunction
Phosphorylation
PRDX2 activity is modulated by phosphorylation:
- Casein kinase 2 (CK2) phosphorylates PRDX2
- Tyrosine kinases can modify PRDX2
- Phosphorylation affects oligomerization dynamics
Molecular Interactions
Protein-Protein Interactions
PRDX2 interacts with numerous proteins that modulate its function:
| Interactor | Interaction Type | Functional Consequence |
|------------|------------------|------------------------|
| Thioredoxin (Trx) | Substrate provider | Reduces PRDX2 disulfide for regeneration |
| Thioredoxin Reductase (TrxR) | Indirect | Maintains Trx in reduced state |
| ASK1 | Binding partner | Releases upon oxidation to activate JNK pathway |
| JNK | Downstream kinase | Pro-apoptotic signaling when activated |
| p38 MAPK | Interaction | Stress-responsive signaling |
| Vimentin | Binding | Cytoskeletal protection |
| Alpha-synuclein | Colocalization | May seed or inhibit aggregation |
| Amyloid-beta | Interaction | Protection against oxidative damage |
| SOD1 | Co-expression | Synergistic antioxidant defense |
Signaling Pathway Integration
PRDX2 integrates with several critical cellular signaling pathways:
MAPK/ERK Pathway:
- Oxidized PRDX2 can influence ERK phosphorylation
- Affects cell survival and proliferation decisions
- Cross-talk with growth factor signaling
PI3K/Akt Pathway:
- PRDX2 activity affects Akt phosphorylation status
- Influences cellular survival pathways
- Modulates mitochondrial function
NF-κB Pathway:
- Redox status influences NF-κB activation
- PRDX2 can either promote or inhibit NF-κB depending on context
- Affects inflammatory gene expression
Therapeutic Implications
Therapeutic Strategies
1. PRDX2 Overexpression
- Viral vector delivery of PRDX2 gene (AAV serotypes)
- Small molecule upregulators of PRDX2 expression
- Cell-penetrating PRDX2 peptides
- Gene therapy approaches for direct CNS delivery
2. Enhancement of PRDX2 Activity
- Thioredoxin system enhancers to maintain PRDX2 in reduced state
- Small molecules that prevent PRDX2 hyperoxidation
- Inhibitors of PRDX2-specific oxidases
- Redox buffer compounds
3. Stabilization of PRDX2 Oligomers
- Compounds that promote the chaperone-active decameric form
- Stabilizers of PRDX2's reduced state
- Allosteric modulators of oligomerization
4. Antioxidant Combination Therapies
- PRDX2 with other antioxidant enzymes (SOD, catalase)
- Combined antioxidant and anti-inflammatory approaches
- Mitochondrial-targeted antioxidants
Biomarker Potential
PRDX2 has potential as a biomarker for oxidative stress in neurodegeneration:
- Cerebrospinal fluid: PRDX2 levels can be measured in CSF
- Blood: Extracellular PRDX2 can serve as a biomarker for oxidative stress
- Brain imaging: PET ligands targeting oxidized PRDX2 are under development
- Exosomes: PRDX2 in neuronal exosomes as disease marker
Drug Development Targets
- PRDX2 agonists: Compounds that upregulate or activate PRDX2
- Thioredoxin reductase inhibitors: To maintain thioredoxin in reduced state for PRDX2 regeneration
- Peroxynitrite scavengers: To reduce PRDX2 inactivation by peroxynitrite
- S-nitrosylation modulators: Control of PRDX2 S-nitrosylation
Clinical Translation Challenges
Blood-brain barrier: Delivery of therapeutic agents to CNS
Target engagement: Verifying PRDX2 modulation in vivo
Biomarker validation: Correlating PRDX2 with clinical outcomes
Dosage optimization: Balancing antioxidant effects
Safety concerns: Potential for interfering with redox signalingAnimal Models
Genetic Models
PRDX2 Knockout Mice:
- Viable and fertile with subtle phenotypes
- Increased sensitivity to oxidative stress
- Accelerated aging phenotype
- Accumulation of oxidative damage markers
PRDX2 Transgenic Mice:
- Overexpression protects against various stressors
- Improved outcomes in MPTP models
- Reduced neuroinflammation
- Better cognitive performance with age
Toxin Models
PRDX2 modulation affects outcomes in:
- MPTP model of Parkinson's disease
- 6-OHDA lesion model
- Amyloid-beta infusion models
- Transgenic AD models (APP/PS1, 3xTg-AD)
- Rotenone exposure models
Therapeutic Testing
- AAV-PRDX2 delivery in toxin models
- Small molecule PRDX2 activators
- Thioredoxin system enhancers
- Combined antioxidant approaches
Research Directions
Current Research Areas
Structural studies: Understanding PRDX2's redox-regulated conformational changes
Post-translational modifications: Phosphorylation, acetylation, and nitrosylation effects
Cell-type specific functions: PRDX2's role in different neuronal subtypes
Protein-protein interactions: Network analysis of PRDX2's interaction partnersUnanswered Questions
- How does PRDX2 oxidation specifically contribute to alpha-synuclein aggregation?
- What determines which form (peroxidase vs. chaperone) PRDX2 adopts?
- Can PRDX2-based therapies be delivered effectively to the brain?
- What is the relationship between PRDX2 oxidation and disease progression?
- How do different neuronal populations differ in PRDX2 expression?
Emerging Areas
- Single-cell analysis: PRDX2 expression across neuronal subtypes
- Spatial transcriptomics: Regional vulnerability patterns
- Proteomics: Interaction network mapping
- Small molecule screening: High-throughput discovery of PRDX2 modulators
Interactive Elements
Pathway Diagram
Mermaid diagram (expand to render)
Summary Table
| Feature | Normal Neuron | Neurodegeneration |
|---------|---------------|-------------------|
| PRDX2 oxidation | Low | High |
| Oligomerization | Transient | Sustained |
| Chaperone activity | inducible | overwhelmed |
| Thioredoxin system | functional | compromised |
| Cell survival | maintained | impaired |
Clinical Perspectives
Diagnostic Applications
PRDX2 measurement offers valuable insights into neurodegenerative disease diagnostics:
Cerebrospinal Fluid (CSF) Analysis:
- PRDX2 levels elevated in PD and AD patients
- Correlation with disease severity and progression
- Potential for differential diagnosis
- Combination with other biomarkers
Blood-Based Biomarkers:
- Peripheral blood mononuclear cell (PBMC) PRDX2
- Serum PRDX2 as oxidative stress marker
- Exosome-associated PRDX2
- Longitudinal monitoring potential
Imaging Correlations:
- MRI-based oxidative stress markers
- PET tracer development for oxidized proteins
- Correlation with regional atrophy patterns
Therapeutic Monitoring
PRDX2 as a therapeutic target requires monitoring:
Target Engagement:
- Measuring PRDX2 oxidation status
- Tracking oligomerization changes
- Assessing chaperone activity
- Evaluating thioredoxin system function
Clinical Endpoints:
- Cognitive function assessments
- Motor function evaluations
- Quality of life measures
- Biomarker correlations
Comparative Biology
Evolutionary Conservation
PRDX2 is highly conserved across species:
| Species | Sequence Identity | Functional Conservation |
|---------|-------------------|-------------------------|
| Human | 100% | Complete |
| Mouse | 98% | Full function |
| Zebrafish | 85% | High conservation |
| Drosophila | 72% | Partial function |
| C. elegans | 65% | Peroxidase activity |
Species-Specific Studies
Rodent Models:
- Mouse models show age-related PRDX2 changes
- Rat primary neuron cultures
- Behavioral correlates of PRDX2 status
Lower Organisms:
- Drosophila melanogaster studies
- Zebrafish neuronal development
- C. elegans oxidative stress response
Background
The study of Prdx2 — Peroxiredoxin 2 has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions. The dual functionality of PRDX2 as both peroxidase and molecular chaperone makes it uniquely positioned to protect neurons from the combined challenges of oxidative stress and protein aggregation that characterize neurodegenerative diseases.
See Also
- Peroxiredoxins
- [Oxidative Stress](/mechanisms/oxidative-stress)
- [Thioredoxin](/genes/txn)
- [Alpha-Synuclein](/proteins/alpha-synuclein)
- [Parkinson's Disease Mechanisms](/diseases/parkinsons-disease)
- [Alzheimer's Disease Molecular Mechanisms](/diseases/alzheimers-disease)
- [Neuroprotection](/treatments/neuroprotection)
External Links
- [NCBI Gene: PRDX2](https://www.ncbi.nlm.nih.gov/gene/7003)
- [UniProt: PRDX2](https://www.uniprot.org/uniprot/P32189)
- [Ensembl: PRDX2](https://ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000167612)
- [OMIM: PRDX2](https://omim.org/entry/607386)
References
[Lee et al., Peroxiredoxin function in oxidative stress response and signaling (2011)](https://pubmed.ncbi.nlm.nih.gov/20812876/)
[Tasset et al., Redox imbalance in neurodegenerative diseases (2012)](https://pubmed.ncbi.nlm.nih.gov/22324453/)
[Klammer et al., Structural and functional analysis of peroxiredoxin 2 (2020)](https://pubmed.ncbi.nlm.nih.gov/32871324/)
[Kim et al., Peroxiredoxin family in cellular antioxidant defense (2008)](https://pubmed.ncbi.nlm.nih.gov/18687751/)
[Riso et al., Oxidative stress triggers peroxiredoxin oligomerization (2009)](https://pubmed.ncbi.nlm.nih.gov/19496350/)
[Wang et al., Crystal structure of human peroxiredoxin 2 (2014)](https://pubmed.ncbi.nlm.nih.gov/25146837/)
[Yang et al., Catalytic mechanism of 2-Cys peroxiredoxins (2009)](https://pubmed.ncbi.nlm.nih.gov/19318436/)
[Hu et al., Peroxiredoxin 2 oligomerization and chaperone function (2009)](https://pubmed.ncbi.nlm.nih.gov/19240134/)
[Mann et al., Peroxiredoxin 2 in neuronal antioxidant defense (2006)](https://pubmed.ncbi.nlm.nih.gov/16507885/)
[Fujii et al., Peroxiredoxin as molecular chaperone under oxidative stress (2010)](https://pubmed.ncbi.nlm.nih.gov/20053993/)
[Yang et al., Regulation of apoptosis by peroxiredoxin 2 (2007)](https://pubmed.ncbi.nlm.nih.gov/17213082/)
[Eng et al., Peroxiredoxin 2 protects dopaminergic neurons from oxidative stress (2015)](https://pubmed.ncbi.nlm.nih.gov/25664856/)
[Ng et al., Mitochondrial peroxiredoxin 2 function (2016)](https://pubmed.ncbi.nlm.nih.gov/26922875/)
[Perez et al., Peroxiredoxin 2 oxidation in Parkinson's disease substantia nigra (2018)](https://pubmed.ncbi.nlm.nih.gov/29953882/)
[Kim et al., Peroxiredoxin 2 in Alzheimer's disease pathogenesis (2019)](https://pubmed.ncbi.nlm.nih.gov/30659468/)
[Yang et al., Peroxiredoxin 2 in amyotrophic lateral sclerosis (2020)](https://pubmed.ncbi.nlm.nih.gov/32042189/)
[Chen et al., Peroxiredoxin 2 neuroprotection in cerebral ischemia (2019)](https://pubmed.ncbi.nlm.nih.gov/31028727/)
[Liu et al., Peroxiredoxin 2 and alpha-synuclein aggregation (2018)](https://pubmed.ncbi.nlm.nih.gov/29505921/)
[Zhang et al., Thioredoxin-peroxiredoxin system in neurodegeneration (2017)](https://pubmed.ncbi.nlm.nih.gov/28548096/)
[Ahmad et al., Peroxiredoxin as therapeutic target in neurodegeneration (2013)](https://pubmed.ncbi.nlm.nih.gov/24095595/)
[Nagai et al., Peroxiredoxin 2 regulates ferroptosis in dopaminergic neurons (2019)](https://pubmed.ncbi.nlm.nih.gov/31197176/)
[Kar et al., Peroxiredoxin 2 and neuroinflammation in Parkinson's disease (2018)](https://pubmed.ncbi.nlm.nih.gov/29654658/)
[Ma et al., Peroxiredoxin 2 post-translational modifications in aging brain (2019)](https://pubmed.ncbi.nlm.nih.gov/31124297/)
[Thomson et al., Regulation of peroxiredoxin by reversible oxidation (2015)](https://pubmed.ncbi.nlm.nih.gov/25866810/)Pathway Diagram
The following diagram shows the key molecular relationships involving PRDX2 — Peroxiredoxin 2 discovered through SciDEX knowledge graph analysis:
Mermaid diagram (expand to render)