Affinage

PRDX5

Peroxiredoxin-5, mitochondrial · UniProt P30044

Length
214 aa
Mass
22.1 kDa
Annotated
2026-06-10
44 papers in source corpus 17 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PRDX5 is a thiol-dependent peroxiredoxin antioxidant enzyme that scavenges hydrogen peroxide and alkyl hydroperoxides through a thiol-specific catalytic mechanism, providing antioxidant protection comparable to catalase in vitro (PMID:10521424, PMID:10514471). It is dually targeted to mitochondria and peroxisomes, with N- and C-terminal targeting determinants directing organellar sorting; peroxisomal import depends on a C-terminal SQL tripeptide that is necessary and sufficient for recognition by the PTS1 receptor PEX5 (PMID:10521424, PMID:10514471). Its peroxidase activity is the basis of its cytoprotective functions: recombinant enzyme requires intact peroxidase activity for anti-inflammatory effects in macrophages (PMID:35985565), and its antioxidant and anti-apoptotic outputs are negatively regulated by acetylation, such that increasing PRDX5 acetylation elevates ROS and apoptosis while deacetylation is protective (PMID:41740330). PRDX5 supports mitochondrial homeostasis by binding TFAM and acting upstream of TFAM-mediated mitochondrial function (PMID:39955823), and during myogenesis it promotes mitochondrial transport and myonuclear positioning through transcriptional regulation of Rhot1 and Trak1, with mitochondrial ATP production reduced upon its loss (PMID:41147088). In oxidative-stress and cancer contexts PRDX5 physically interacts with Nrf2 to promote NQO1 expression and drug resistance (PMID:31899687, PMID:37305326, PMID:39168191), regulates the DNA damage response via Plk1–ATM–Chek1/2 signaling and Sirt2-dependent p53 acetylation (PMID:36067023), drives ROS-dependent M1 macrophage polarization through TLR4/NF-κB (PMID:40015209), and protects against ferroptosis by potentiating SLC7A11/GPX4 (PMID:40654183). PRDX5 expression is transcriptionally activated by STAT3 binding to its promoter, an interaction enhanced by ROS-mediated promoter demethylation (PMID:33416106).

Mechanistic history

Synthesis pass · year-by-year structured walk · 9 steps
  1. 1999 High

    Established that PRDX5 is a bona fide antioxidant enzyme, defining its core biochemical identity as a thiol-dependent peroxidase rather than an inferred family member.

    Evidence Recombinant E. coli protein with in vitro peroxidase and glutamine synthetase protection assays distinguishing thiol-specific from non-thiol activity

    PMID:10514471 PMID:10521424

    Open questions at the time
    • Catalytic cysteine residues and regeneration mechanism not resolved in these assays
    • Physiological substrate spectrum beyond H2O2 not delimited
  2. 1999 High

    Resolved how PRDX5 reaches its sites of action, showing dual mitochondrial/peroxisomal targeting and defining the molecular import determinant for peroxisomes.

    Evidence GFP fusion live-cell imaging in HepG2 cells plus direct PMP20–PEX5 binding assay with SQL mutagenesis, fractionation, and thiolase co-localization

    PMID:10514471 PMID:10521424

    Open questions at the time
    • Mitochondrial targeting sequence not mapped at residue resolution
    • Determinants partitioning the protein between the two organelles not defined
  3. 2014 Medium

    Demonstrated PRDX5 is structurally druggable, identifying distinct ligand-binding pockets to guide small-molecule modulation.

    Evidence Ligand-observed STD NMR and protein-observed 15N-HSQC chemical shift perturbation fragment mapping

    PMID:25025339

    Open questions at the time
    • No functional consequence of fragment binding established
    • Binding sites not linked to catalytic regulation
  4. 2020 Medium

    Connected PRDX5 to redox-responsive transcriptional programs, showing it both interacts with Nrf2 to drive NQO1 and is itself a STAT3 target under ROS-modulated epigenetic control.

    Evidence Co-IP in H2O2-stimulated NSCLC cells; ChIP, luciferase reporter, bisulfite sequencing, and STAT3 loss/gain-of-function

    PMID:31899687 PMID:33416106

    Open questions at the time
    • Whether PRDX5–Nrf2 interaction is direct not established by reciprocal/structural validation
    • Functional link between PRDX5 peroxidase activity and Nrf2 stabilization not mechanistically resolved
  5. 2023 Medium

    Placed PRDX5 within DNA damage response signaling and as a stable Nrf2 complex partner driving tumor cell proliferation and drug resistance.

    Evidence Prdx5 knockdown with γ-H2AX/53BP1, ATM phosphorylation and p53 acetylation readouts, Sirt2 deacetylase identification; Co-IP plus zebrafish xenografts

    PMID:36067023 PMID:37305326

    Open questions at the time
    • Direct biochemical link between PRDX5 enzymatic activity and Plk1–ATM axis not reconstituted
    • Stoichiometry and interface of the PRDX5–Nrf2 complex undefined
  6. 2025 High

    Defined non-classical, structural and trafficking roles for PRDX5 in mitochondrial biology, linking it to TFAM-dependent mitochondrial homeostasis and to Rhot1/Trak1-mediated mitochondrial transport and myonuclear positioning.

    Evidence PRDX5–TFAM binding assay with TFAM knockdown rescue in CKD models; Prdx5-/- myotube Seahorse, super-resolution SIM, and Rhot1/Trak1 knockdown epistasis

    PMID:39955823 PMID:41147088

    Open questions at the time
    • Mechanism by which PRDX5 transcriptionally controls Rhot1/Trak1 unknown
    • Whether TFAM binding is direct and how it modulates TFAM function not structurally resolved
  7. 2025 Medium

    Established acetylation as a key negative regulatory switch on PRDX5 antioxidant function, integrated within SIRT3/SIRT2 deacetylase axes governing neuroprotection.

    Evidence OGD/R retinal model with pharmacological acetylation manipulation (NAM/NRC) and PRDX5 over/knockdown; SIRT3-PRDX5 co-localization and genetic epistasis in SCI model

    PMID:40818507 PMID:41740330

    Open questions at the time
    • Specific acetylated lysine residues on PRDX5 not mapped
    • Direct deacetylase–substrate biochemistry not demonstrated
  8. 2025 Medium

    Extended PRDX5 cytoprotective output to ferroptosis defense and immune/inflammatory regulation, and identified its regulation by upstream IER3–PARL-controlled mitochondrial translocation.

    Evidence SAB target engagement (DARTS, CETSA, docking) with SLC7A11/GPX4 readouts; TLR4/NF-κB macrophage polarization with siRNA; IER3 knockout RNA-seq, IER3–PARL Co-IP, and mitochondrial fractionation

    PMID:40015209 PMID:40654183 PMID:41359162

    Open questions at the time
    • Direct molecular link between PRDX5 redox activity and GPX4/SLC7A11 not established
    • PARL cleavage site on PRDX5 not mapped
  9. 2025 Low

    Raised the possibility of a peroxidase-to-chaperone functional switch via oxidative-stress-induced oligomerization and extracellular/exosomal trafficking.

    Evidence Imaging flow cytometry, native/denaturing PAGE, and fluorescence microscopy in cryopreserved bull sperm

    PMID:39780184

    Open questions at the time
    • TLR4 interaction proposed but not demonstrated by Co-IP
    • Chaperone activity of oligomers not biochemically confirmed
    • Single descriptive study in one model system

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single peroxidase coordinates its many divergent roles — organellar antioxidant catalysis, transcriptional control of mitochondrial transport, protein-complex scaffolding with Nrf2 and TFAM, and putative chaperone activity — through shared structural and regulatory determinants remains unresolved.
  • No structural model linking catalytic state to interaction partners
  • Mechanism converting enzymatic activity into transcriptional regulation of Rhot1/Trak1 unknown
  • Tissue-specific determinants of which PRDX5 function dominates not defined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016491 oxidoreductase activity 3 GO:0016209 antioxidant activity 2 GO:0140098 catalytic activity, acting on RNA 2
Localization
GO:0005739 mitochondrion 3 GO:0005777 peroxisome 2 GO:0005829 cytosol 1
Pathway
R-HSA-8953897 Cellular responses to stimuli 3 R-HSA-168256 Immune System 2 R-HSA-73894 DNA Repair 1
Partners
NFE2L2PARLPEX5TFAMTLR4

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 AOEB166 (PRDX5) is a peroxiredoxin-family antioxidant enzyme with demonstrated peroxidase activity in vitro; recombinant protein expressed in E. coli exhibits peroxidase activity and antioxidant activity comparable to catalase in a glutamine synthetase protection assay against DTT/Fe3+/O2 oxidation. Recombinant protein expression in E. coli, in vitro peroxidase assay, glutamine synthetase protection assay The Journal of biological chemistry High 10521424
1999 AOEB166 (PRDX5) localizes to mitochondria and peroxisomes in HepG2 cells, as shown by GFP fusion protein sorting to both organelles; N- and C-terminal domains contain mitochondrial and peroxisomal targeting sequences. GFP fusion protein expression and fluorescence microscopy in HepG2 cells The Journal of biological chemistry Medium 10521424
1999 Human PMP20 (PRDX5) is imported into the peroxisomal matrix via the PTS1 receptor PEX5; the C-terminal tripeptide SQL is necessary and sufficient for binding to HsPEX5, as shown by direct binding assay and mutagenesis of the SQL sequence. Direct binding assay (PMP20 to HsPEX5), mutagenesis of C-terminal SQL tripeptide, subcellular fractionation, double-staining immunofluorescence co-localization with thiolase The Journal of biological chemistry High 10514471
1999 Human PMP20 (PRDX5) exhibits thiol-specific antioxidant activity (inhibits glutamine synthetase inactivation in thiol-metal-catalyzed but not non-thiol metal-catalyzed oxidation) and thiol-peroxidase activity (removes hydrogen peroxide). In vitro glutamine synthetase protection assay (thiol vs. non-thiol MCO systems), thiol-peroxidase activity assay The Journal of biological chemistry High 10514471
2014 Small-molecule fragments bind to PRDX5 at defined sites; NMR methods (STD-epitope mapping, 15N-HSQC chemical shift perturbation) were used to compare binding modes of analogous fragments, validating PRDX5 as a druggable target with structurally distinct binding pockets. Ligand-observed STD NMR, protein-observed 15N-HSQC NMR, CSP analysis PloS one Medium 25025339
2020 PRDX5 physically interacts with Nrf2 in H2O2-stimulated NSCLC cells, and this interaction promotes NQO1 protein expression; the interaction was detected by co-immunoprecipitation. Co-immunoprecipitation in H2O2-stimulated NSCLC cells, western blot for NQO1 Aging Medium 31899687
2020 STAT3 binds to two specific sites in the PRDX5 promoter (site 1: −444 to −434 bp; site 4: −1,417 to −1,407 bp) and transcriptionally activates PRDX5 expression; ROS-mediated demethylation of the PRDX5 promoter enhances STAT3 binding affinity. Chromatin immunoprecipitation (ChIP), luciferase reporter assay, bisulfite sequencing PCR, STAT3 knockdown/overexpression with western blot International journal of molecular medicine Medium 33416106
2020 PRDX5 overexpression in NSCLC cells under oxidative stress promotes epithelial-mesenchymal transition (decreases E-cadherin, increases vimentin) and activates the Nrf2 signaling pathway, while PRDX5 knockdown has the opposite effects. siRNA knockdown and pcDNA3.1 overexpression, western blot for EMT markers and Nrf2 pathway components in H1299 cells pretreated with H2O2 International journal of molecular medicine Medium 33416106
2023 Prdx5 regulates DNA damage response (DDR) through: (1) Plk1-mediated phosphorylation of ATM kinase activating downstream Chek1/Chek2; (2) increasing p53 acetylation at K382, stabilizing nuclear p53 and enhancing transcription; (3) induction of autophagy that regulates recycling of DDR molecules. Sirt2 was identified as a novel deacetylase of p53 at K382, acting in a Prdx5-dependent manner. Prdx5 knockdown (γ-H2AX and 53BP1 induction), western blot for ATM phosphorylation/Chek1/Chek2, p53 acetylation assays, autophagy induction assays, Sirt2 deacetylase identification Human molecular genetics Medium 36067023
2023 PRDX5 and Nrf2 form a protein complex (confirmed by Co-IP), and their synergistic interaction increases proliferation and drug resistance of NSCLC cells; oxidative stress enhances the PRDX5–Nrf2 interaction. Co-immunoprecipitation, western blotting, immunohistochemistry, zebrafish xenograft models Oncology research Medium 37305326
2025 PRDX5 directly binds TFAM; PRDX5 overexpression enhances TFAM-mediated mitochondrial function, and TFAM knockdown reverses the mitochondrial functional improvements achieved through PRDX5 overexpression, placing PRDX5 upstream of TFAM in mitochondrial homeostasis. Protein binding assay (PRDX5–TFAM interaction), TFAM knockdown rescue experiment, in vitro and in vivo CKD models with PRDX5 overexpression Phytomedicine Medium 39955823
2025 IER3 interacts with the presenilin-associated rhomboid-like protein (PARL) and reduces its shear activity, thereby inhibiting cleavage and mitochondrial translocation of cytoplasmic PRDX5. Reduced mitochondrial PRDX5 impairs antioxidant capacity, causes oxidative mitochondrial damage, and promotes stress-induced cellular senescence driving AKI-to-CKD transition. IER3 knockout mouse RNA-seq identifying PRDX5 upregulation, co-IP of IER3–PARL interaction, PRDX5 inhibition epistasis experiments, mitochondrial fractionation Cellular and molecular life sciences Medium 41359162
2025 SIRT3 promotes PRDX5 function downstream in a SIRT3–PRDX5 axis in spinal cord neurons; SIRT3 and PRDX5 co-localize within neurons of the anterior horn of the spinal cord, and genetic silencing of PRDX5 partially abrogates SIRT3's neuroprotective effects against apoptosis and oxidative stress after spinal cord injury. Transcriptome analysis of Sirt3-/- renal tissues, immunofluorescence co-localization, PRDX5 genetic silencing epistasis experiment in SCI mouse model Brain research bulletin Medium 40818507
2025 Acetylation of PRDX5 inhibits its antioxidant and anti-apoptotic functions in retinal neurons under ischemia-reperfusion: OGD/R increases PRDX5 acetylation; increasing acetylation (NAM treatment) elevates ROS and apoptosis, while decreasing acetylation (NRC treatment) reduces ROS and apoptosis; inhibiting deacetylation abolishes the protective effect of PRDX5 overexpression. OGD/R cell model, pharmacological manipulation of acetylation (NAM/NRC), PRDX5 overexpression/knockdown, ROS assay, apoptosis assay (TUNEL, PI staining), western blot Tissue & cell Medium 41740330
2025 Salvianolic acid B (SAB) directly binds PRDX5 (confirmed by DARTS, CETSA, and molecular docking) and enhances its redox activity, which in turn potentiates SLC7A11 and GPX4 inhibitory effects on ferroptosis; PRDX5 silencing partially abrogates SAB's renoprotective effects in AKI models. DARTS assay, CETSA, molecular docking, PRDX5 knockdown rescue in cisplatin-induced AKI model, in vivo mouse AKI models FASEB journal Medium 40654183
2025 PRDX5 loss-of-function during myogenesis causes myonuclear clustering (impaired nuclear spreading) and reduced mitochondrial ATP production. PRDX5 facilitates mitochondrial transport and nuclear positioning at least in part through transcriptional regulation of Rhot1 and Trak1; knockdown of Rhot1 or Trak1 in WT myotubes phenocopies Prdx5 deficiency. Prdx5-/- mouse myotube analysis, Seahorse OCR mitochondrial function assay, confocal and super-resolution SIM microscopy, Rhot1/Trak1 knockdown epistasis, in vivo muscle function and histology Journal of cachexia, sarcopenia and muscle High 41147088
2025 Prdx5 regulates macrophage polarization toward M1 phenotype in an ROS-dependent manner via the TLR4/NF-κB pathway; Prdx5 silencing suppresses M1 polarization and reduces prostate epithelial cell apoptosis in an experimental autoimmune prostatitis model. siRNA knockdown of Prdx5, western blot, RT-qPCR, flow cytometry, immunofluorescence, immunohistochemistry, cell co-culture, EAP mouse model International immunopharmacology Medium 40015209
2025 Under cryopreservation-induced oxidative stress, PRDX5 translocates intracellularly in bull sperm and forms high-molecular-weight oligomers detected by PAGE; oligomerization may shift PRDX5 function from peroxidase to chaperone. PRDX5 interaction with TLR4 may be key to its intracellular transport, and PRDX5 was detected in exosomal vesicles. Imaging Flow Cytometry, native and denaturing PAGE, fluorescence microscopy, ROS/NO measurement Cell communication and signaling Low 39780184
2024 Stachyose (STA) and its derivative C6-STA inhibit PRDX5 enzymatic activity and disrupt PRDX5–NRF2 protein–protein interaction, leading to decreased NQO1 levels and quinone radical accumulation that induces apoptosis of drug-tolerant persister cells in CRPC. PRDX5 enzyme activity assay, Co-IP (PRDX5–NRF2 interaction), western blot for NQO1, pharmacokinetic analysis, in vitro and in vivo CRPC models International journal of biological macromolecules Medium 39168191
2022 Porcine PRDX5 anti-inflammatory activity depends on its peroxidase activity; recombinant pPRDX5 inhibits TNF-α- and PRRSV-induced inflammatory responses in alveolar macrophages, while siRNA knockdown enhances inflammation. Peroxidase activity is required for the anti-inflammatory effect. Recombinant protein treatment, siRNA knockdown in porcine alveolar macrophages, inflammatory cytokine measurement, peroxidase activity assay Developmental and comparative immunology Medium 35985565

Source papers

Stage 0 corpus · 44 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. The Journal of biological chemistry 210 10521424
1997 Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Yeast (Chichester, England) 156 9234670
1997 Identification of the yeast ACR1 gene product as a succinate-fumarate transporter essential for growth on ethanol or acetate. FEBS letters 125 9395087
1999 Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro. The Journal of biological chemistry 98 10514471
2005 Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis. The Journal of biological chemistry 88 16046399
1992 ACR1, a yeast ATF/CREB repressor. Molecular and cellular biology 73 1448073
2008 Absence of the peroxiredoxin Pmp20 causes peroxisomal protein leakage and necrotic cell death. Free radical biology & medicine 47 18694816
2013 Latency-associated protein Acr1 impairs dendritic cell maturation and functionality: a possible mechanism of immune evasion by Mycobacterium tuberculosis. The Journal of infectious diseases 41 24218502
1994 ACR1, a gene encoding a protein related to mitochondrial carriers, is essential for acetyl-CoA synthetase activity in Saccharomyces cerevisiae. Molecular & general genetics : MGG 37 7908717
2020 PRDX5 as a novel binding partner in Nrf2-mediated NSCLC progression under oxidative stress. Aging 31 31899687
2016 Proteomonas sulcata ACR1: A Fast Anion Channelrhodopsin. Photochemistry and photobiology 27 26686819
2020 PCAT6 mediates cellular biological functions in gastrointestinal stromal tumor via upregulation of PRDX5 and activation of Wnt pathway. Molecular carcinogenesis 19 32339330
2014 Comparing binding modes of analogous fragments using NMR in fragment-based drug design: application to PRDX5. PloS one 18 25025339
2020 ROS‑mediated hypomethylation of PRDX5 promotes STAT3 binding and activates the Nrf2 signaling pathway in NSCLC. International journal of molecular medicine 17 33416106
2010 Comparative proteome profile during the early period of small-for-size liver transplantation in rats revealed the protective role of Prdx5. Journal of hepatology 17 20451279
2023 Identification of PRDX5 as A Target for The Treatment of Castration-Resistant Prostate Cancer. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 14 38115765
2017 Diametric Role of the Latency-Associated Protein Acr1 of Mycobacterium tuberculosis in Modulating the Functionality of Pre- and Post-maturational Stages of Dendritic Cells. Frontiers in immunology 13 28611779
2023 Prdx5 regulates DNA damage response through autophagy-dependent Sirt2-p53 axis. Human molecular genetics 12 36067023
2023 The synergistic effects of PRDX5 and Nrf2 on lung cancer progression and drug resistance under oxidative stress in the zebrafish models. Oncology research 11 37305326
2025 Chaihuang Yishen Granule ameliorates mitochondrial homeostasis by upregulating PRDX5/TFAM axis to inhibit renal fibrosis in CKD. Phytomedicine : international journal of phytotherapy and phytopharmacology 9 39955823
2023 Maresin1 ameliorates MSU crystal-induced inflammation by upregulating Prdx5 expression. Molecular medicine (Cambridge, Mass.) 8 37996809
2006 A multidrug-resistant, acr1-deficient clinical isolate of Mycobacterium tuberculosis is unimpaired for replication in macrophages. The Journal of infectious diseases 8 16703514
1999 Multiple regulatory elements control the expression of the yeast ACR1 gene. FEBS letters 8 10094465
2002 [The BCL-xL and ACR-1 genes promote differentiation and reduce apoptosis in muscle fibers of mdx mice]. Genetika 7 12500669
2018 Mycobacterium tuberculosis host cell interaction: Role of latency associated protein Acr-1 in differential modulation of macrophages. PloS one 6 30395609
2025 Salvianolic Acid B Attenuates Ferroptosis in Acute Kidney Injury by Targeting PRDX5. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 5 40654183
2025 PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress. Cell communication and signaling : CCS 4 39780184
2025 Elevated serum levels of GPX4, NDUFS4, PRDX5, and TXNRD2 as predictive biomarkers for castration resistance in prostate cancer patients: an exploratory study. British journal of cancer 4 39900986
2025 Prdx5 regulates macrophage polarization by modulating the TLR4/NF-κB pathway to promote apoptosis in chronic prostatitis. International immunopharmacology 4 40015209
2024 A novel strategy to elicit enduring anti-morphine immunity and relief from addiction by targeting Acr1 protein nano vaccine through TLR-2 to dendritic cells. International journal of biological macromolecules 4 38880456
2022 Molecular cloning, prokaryotic expression and the anti-inflammatory activity of porcine PRDX5. Developmental and comparative immunology 4 35985565
2025 Single-cell sequencing combined with urinary multi-omics analysis reveals that the non-invasive biomarker PRDX5 regulates bladder cancer progression through ferroptosis signaling. BMC cancer 3 40122834
2025 F18 Promiscuous Epitope of Acr1 Protein of Mycobacterium tuberculosis Induces the Secretion of IL-10 and Tregs but Not IL-6. Protein and peptide letters 3 40798978
2024 First report of Peroxiredoxin-5 (PRDX5) in starry flounder (Platichthys stellatus): Molecular features and expression analysis. Developmental and comparative immunology 3 39571926
2025 PRDX5 Regulates Mitochondrial Function and Nuclear Spreading in Myogenesis and Acts With PRDX3 to Delay Muscle Aging. Journal of cachexia, sarcopenia and muscle 2 41147088
2024 Prebiotic stachyose inhibits PRDX5 activity and castration-resistant prostate cancer development. International journal of biological macromolecules 2 39168191
2026 CD133+ Lung Cancer Stem-like Cells Resist Plasma-activated Medium Through PRDX5-mediated Antioxidant Defense. Anticancer research 1 41760234
2025 Activation of SIRT3 / PRDX5 signaling inhibits apoptosis after acute spinal cord injury in mice. Brain research bulletin 1 40818507
2023 Prdx5 in the Regulation of Tuberous Sclerosis Complex Mutation-Induced Signaling Mechanisms. Cells 1 37443747
2026 Acetylation of PRDX5 aggravates the oxidative stress and apoptosis of retinal neurons induced by ischemia-reperfusion. Tissue & cell 0 41740330
2025 Ethyl β-carboline-3-carboxylate targets PRDX5/c-Jun axis for novel therapeutic strategy against cervical cancer. Discover oncology 0 40775543
2025 Mycobacterium tuberculosis Acr1 Protein Mitigates Experimental Autoimmune Encephalomyelitis Symptoms by Generating Myeloid-Derived Suppressor Cells and Regulatory T Cells. Immunology 0 41111357
2025 IER3 drives the transition from sepsis-associated AKI to CKD by suppressing the mitochondrial translocation of PRDX5. Cellular and molecular life sciences : CMLS 0 41359162
2016 Association between ACR1 gene product expression and cardiomyopathy in children. Experimental and therapeutic medicine 0 27588091

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