Affinage

PRDX5

Peroxiredoxin-5, mitochondrial · UniProt P30044

Round 2 corrected
Length
214 aa
Mass
22.1 kDa
Annotated
2026-04-28
74 papers in source corpus 24 papers cited in narrative 24 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PRDX5 is the sole mammalian atypical 2-Cys peroxiredoxin, functioning as a broad-spectrum peroxidase that reduces alkyl hydroperoxides, H₂O₂, and peroxynitrite (rate constant ~10⁷ M⁻¹s⁻¹) through a catalytic cycle in which the peroxidatic Cys47 is oxidized to sulfenic acid, forms an intramolecular disulfide with the resolving Cys152 (separated by 13.8 Å in the reduced crystal structure, requiring conformational change), and is recycled by thioredoxin (PMID:10751410, PMID:11518528, PMID:15280035). Distributed across mitochondria, peroxisomes, cytosol, and nucleus via distinct targeting sequences, PRDX5 protects cells from nitro-oxidative stress and suppresses TNF-α–induced JNK activation and p53-induced apoptosis; its mitochondrial import is controlled by IER3 through the Parl protease, and its activity is negatively regulated by acetylation (PMID:10521424, PMID:10751410, PMID:41359162, PMID:41740330). Beyond canonical antioxidant defense, PRDX5 physically interacts with Nrf2 to promote NQO1 expression and drug resistance in cancer, operates downstream of SIRT3 in neuroprotection, modulates M1 macrophage polarization via TLR4/NF-κB, regulates the DNA damage response through the ATM/Plk1/Sirt2/p53 axis, and coordinates mitochondrial transport and myonuclear positioning during myogenesis through transcriptional regulation of Rhot1 and Trak1 (PMID:31899687, PMID:36067023, PMID:40818507, PMID:40015209, PMID:41147088). PRDX5 upregulation in drug-tolerant persister cells promotes castration-resistant prostate cancer, and disruption of its interaction with NRF2 restores drug sensitivity (PMID:38115765, PMID:39168191).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 1999 High

    Identification of PRDX5 as a novel mammalian peroxiredoxin with dual mitochondrial and peroxisomal targeting established that mammals possess a peroxiredoxin distinct from the known typical 2-Cys family members, with peroxisomal import mediated by PTS1 signal recognition by PEX5.

    Evidence Recombinant expression, GFP-fusion localization in HepG2, PEX5 binding assays with PTS1 mutagenesis

    PMID:10514471 PMID:10521424

    Open questions at the time
    • Cytosolic and nuclear targeting mechanisms not yet defined
    • Endogenous substrates in each compartment unknown
  2. 2000 High

    Defining the atypical 2-Cys catalytic mechanism — intramolecular disulfide between Cys48 and Cys152, recycled by thioredoxin but not glutaredoxin — resolved how PRDX5 differs mechanistically from all other mammalian peroxiredoxins and established its first cellular function: suppression of TNF-α–induced JNK activation and p53-induced apoptosis.

    Evidence Site-directed mutagenesis of each Cys, thioredoxin-dependent peroxidase assays, overexpression in NIH 3T3 (JNK readout) and mammalian cells (p53-apoptosis readout)

    PMID:10679306 PMID:10751410

    Open questions at the time
    • Structural basis for intramolecular disulfide formation not yet available
    • Mechanism of p53-apoptosis inhibition beyond ROS scavenging unclear
  3. 2001 High

    The 1.5 Å crystal structure of reduced PRDX5 revealed a thioredoxin-fold monomer with 13.8 Å separation between catalytic cysteines, demonstrating that a major conformational change must accompany oxidation — explaining why the enzyme is monomeric rather than forming the obligate dimers seen in typical 2-Cys peroxiredoxins.

    Evidence X-ray crystallography at 1.5 Å resolution

    PMID:11518528

    Open questions at the time
    • Oxidized-form structure not captured
    • Conformational dynamics during catalysis unresolved
  4. 2004 High

    Pulse radiolysis measurement of the peroxynitrite reduction rate constant (~7×10⁷ M⁻¹s⁻¹) established PRDX5 as one of the fastest biological peroxynitrite reductases, expanding its functional role from H₂O₂ scavenging to reactive nitrogen species defense.

    Evidence Pulse radiolysis kinetics with Cys mutants

    PMID:15280035

    Open questions at the time
    • Relative contribution to peroxynitrite scavenging in vivo versus other reductases untested
    • Compartment-specific kinetics not measured
  5. 2010 Medium

    In vivo gain-of-function via adenoviral PRDX5 overexpression in rat liver transplantation demonstrated that PRDX5 protects against ischemia-reperfusion injury, extending its antioxidant role to a whole-organ pathological context.

    Evidence Adenoviral overexpression in small-for-size rat liver grafts with survival analysis

    PMID:20451279

    Open questions at the time
    • Downstream signaling pathway mediating hepatoprotection not defined
    • Loss-of-function in this model not performed
  6. 2020 Medium

    Discovery of the PRDX5–Nrf2 physical interaction revealed a non-canonical signaling role: PRDX5 promotes NQO1 expression under oxidative stress, and STAT3 transcriptionally upregulates PRDX5 via promoter hypomethylation, positioning PRDX5 within a STAT3→PRDX5→Nrf2 signaling axis that promotes EMT and drug resistance in NSCLC.

    Evidence Co-immunoprecipitation, ChIP for STAT3 binding at PRDX5 promoter, bisulfite sequencing, siRNA/overexpression with EMT markers

    PMID:31899687 PMID:33416106

    Open questions at the time
    • Binding interface between PRDX5 and Nrf2 unmapped
    • Whether PRDX5 redox activity is required for Nrf2 interaction unknown
    • Reciprocal Co-IP for PRDX5–Nrf2 not shown in original report
  7. 2022 Medium

    Porcine PRDX5 demonstrated peroxidase-activity-dependent anti-inflammatory function in macrophages stimulated with TNF-α or PRRSV, providing direct evidence that PRDX5's enzymatic activity (not merely protein presence) underlies its immunomodulatory effects.

    Evidence Recombinant protein treatment and siRNA knockdown in porcine alveolar macrophages with peroxidase activity-dependence assays

    PMID:35985565

    Open questions at the time
    • Mechanism linking peroxidase activity to inflammatory signaling not identified
    • Cross-species generalizability to human macrophages not confirmed
  8. 2023 Medium

    PRDX5 was placed within the DNA damage response pathway operating through ATM/Plk1/Sirt2/p53, with Sirt2 identified as a novel PRDX5-dependent p53 K382 deacetylase, and separately shown to promote castration-resistant prostate cancer via its role in drug-tolerant persister cell survival.

    Evidence siRNA knockdown with γ-H2AX/53BP1 readouts, p53 acetylation assays in Pkd1 mutant cells; PRDX5 inhibition in CRPC animal models

    PMID:36067023 PMID:38115765

    Open questions at the time
    • Direct physical interaction between PRDX5 and Sirt2 not demonstrated
    • How PRDX5 peroxidase activity connects to DDR signaling mechanistically unclear
    • Whether DDR and CRPC roles converge on a shared mechanism unknown
  9. 2024 Medium

    Pharmacological disruption of the PRDX5–NRF2 protein–protein interaction by stachyose validated this complex as a druggable node: inhibiting PRDX5 enzymatic activity and NRF2 binding decreased NQO1 levels and induced apoptosis of drug-resistant persister cells in CRPC models.

    Evidence Enzyme activity assays, interaction disruption assays, NQO1 immunoblotting, apoptosis readout, CRPC mouse pharmacokinetics

    PMID:39168191

    Open questions at the time
    • Structural basis of stachyose–PRDX5 binding undefined
    • Selectivity of stachyose for PRDX5 over other peroxiredoxins untested
  10. 2025 Medium

    Multiple 2025 studies expanded PRDX5 from a simple antioxidant to a multifunctional signaling hub: genetic knockout revealed its requirement for mitochondrial transport (Rhot1/Trak1) and myonuclear positioning during myogenesis; epistasis experiments placed it downstream of SIRT3 in neuroprotection; IER3 was shown to control its mitochondrial import via Parl protease; and acetylation was identified as a direct negative regulator of its activity.

    Evidence Prdx5⁻/⁻ and Prdx3⁻/⁻;Prdx5⁻/⁻ mice with Seahorse/microscopy/Rhot1-Trak1 knockdown; SIRT3 agonist plus PRDX5 siRNA epistasis in SCI model; IER3 KO mice with Co-IP of IER3–Parl; OGD/R with acetylation modulation in retinal neurons; TLR4/NF-κB pathway in macrophage polarization

    PMID:40015209 PMID:40818507 PMID:41147088 PMID:41359162 PMID:41740330

    Open questions at the time
    • Acetylation site(s) on PRDX5 not mapped
    • Whether SIRT3 directly deacetylates PRDX5 not tested
    • How Parl cleavage enables mitochondrial import structurally unresolved
    • Integration of myogenesis and immune roles into a unified regulatory model lacking

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: the identity of the acetyltransferase/deacetylase pair controlling PRDX5 activity, the structural basis of the PRDX5–Nrf2 interaction and whether it requires PRDX5's redox state, the oxidized-form crystal structure capturing the conformational change, and how PRDX5's compartment-specific functions are differentially regulated.
  • No oxidized-state crystal structure available
  • Acetylation sites and modifying enzymes unidentified
  • Compartment-specific knockout or targeting studies lacking
  • PRDX5–Nrf2 binding interface and redox dependence unmapped

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016209 antioxidant activity 6 GO:0016491 oxidoreductase activity 5 GO:0098772 molecular function regulator activity 3
Localization
GO:0005739 mitochondrion 5 GO:0005777 peroxisome 3 GO:0005829 cytosol 2 GO:0005634 nucleus 1
Pathway
R-HSA-8953897 Cellular responses to stimuli 4 R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 2 R-HSA-5357801 Programmed Cell Death 2 R-HSA-73894 DNA Repair 1
Partners
IER3NRF2PARLPEX5SIRT3TFAMTLR4

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 PRDX5 (originally named AOEB166) was identified as a novel mammalian peroxiredoxin with peroxidase activity. Recombinant AOEB166 expressed in E. coli exhibits peroxidase activity and antioxidant activity comparable to catalase. The protein contains both mitochondrial and peroxisomal targeting sequences, and GFP-fusion protein expressed in HepG2 cells is sorted to both organelles. Recombinant protein expression in E. coli, glutamine synthetase protection assay, GFP fusion subcellular localization in HepG2 cells, mRNA distribution analysis The Journal of biological chemistry High 10521424
1999 Human PMP20 (PRDX5 ortholog) localizes to peroxisomes via a C-terminal PTS1 signal (SQL tripeptide) that binds the peroxisomal targeting signal receptor HsPEX5; mutagenesis of the SQL sequence abolishes binding to HsPEX5. HsPMP20 exhibits thiol-specific antioxidant activity (inhibiting glutamine synthetase inactivation in thiol-dependent oxidation system) and thiol-peroxidase activity removing H2O2. Mutagenesis analysis, direct binding assay to HsPEX5, subcellular fractionation, double-staining immunofluorescence, glutamine synthetase protection assay, thiol-peroxidase activity assay The Journal of biological chemistry High 10514471
2000 PrxV (PRDX5) forms an intramolecular disulfide as a reaction intermediate during peroxide reduction, distinguishing it from other peroxiredoxins that form intermolecular disulfides or sulfenic acid intermediates. Cys48 is the peroxidatic site oxidized by peroxides, and oxidized Cys48 reacts with Cys152 to form an intramolecular disulfide. The disulfide is reduced by thioredoxin but not by glutaredoxin or glutathione. PRDX5 is localized to cytosol, mitochondria, and peroxisomes. Overexpression of wild-type but not Cys48 mutant inhibited H2O2 accumulation and c-Jun N-terminal kinase activation induced by TNF-alpha in NIH 3T3 cells. Site-directed mutagenesis of each Cys residue, thioredoxin-dependent peroxidase activity assay, immunoblot analysis of tissue distribution, subcellular localization by fractionation, transient overexpression with H2O2 and JNK activation readouts The Journal of biological chemistry High 10751410
2000 Mouse peroxiredoxin V (PRDX5) is a thioredoxin peroxidase that inhibits p53-induced apoptosis. Overexpression of Prx-V prevented p53-dependent generation of reactive oxygen species and inhibited p53-induced apoptosis in mammalian cells. Overexpression in mammalian cells, ROS measurement, apoptosis assay, thioredoxin peroxidase activity assay Biochemical and biophysical research communications Medium 10679306
2001 The 1.5 Å crystal structure of human PRDX5 in reduced form reveals a thioredoxin-like domain. Unlike other mammalian peroxiredoxins, PRDX5 does not form a homodimer. In the reduced form, the catalytic Cys47 and Cys151 are 13.8 Å apart, indicating a conformational change is required to form the intramolecular disulfide upon oxidation. A benzoate ion was found near the active-site pocket. X-ray crystallography at 1.5 Å resolution Journal of molecular biology High 11518528
2003 PRDX5 is classified as the atypical 2-Cys peroxiredoxin: it uses an active-site cysteine (peroxidatic Cys) oxidized to sulfenic acid by peroxide substrate, then forms an intramolecular disulfide with the resolving Cys, recycled by thioredoxin. This mechanism is distinct from typical 2-Cys Prxs (intermolecular disulfide) and 1-Cys Prxs. Biochemical analysis and crystal structure review; mechanistic classification based on structural and mutational data Trends in biochemical sciences High 12517450
2004 Human PRDX5 is a peroxynitrite reductase. The nucleophilic attack on the O-O bond of peroxynitrite is performed by the N-terminal peroxidatic Cys47. Using pulse radiolysis, the rate constant for peroxynitrite reduction was measured at (7±3)×10^7 M⁻¹s⁻¹, among the highest reported for any peroxynitrite reductase. Cysteine mutant analysis, pulse radiolysis to determine rate constant FEBS letters High 15280035
2011 PRDX5 is the unique atypical 2-Cys peroxiredoxin in mammals, localized to mitochondria, peroxisomes, cytosol, and nucleus. It reduces alkyl hydroperoxides and peroxynitrite using cytosolic or mitochondrial thioredoxins with rate constants of 10^6–10^7 M⁻¹s⁻¹, while reduction of H2O2 is more modest (~10^5 M⁻¹s⁻¹). Overexpression in different subcellular compartments protects cells from nitro-oxidative stress, while gene silencing increases vulnerability. Biochemical kinetic assays, subcellular fractionation, overexpression and knockdown with cell viability readouts (comprehensive review of accumulated experimental data) Antioxidants & redox signaling High 20977338
2010 Prdx5 overexpression via adenoviral vector in small-for-size liver grafts during transplantation attenuated graft injury and increased recipient survival, demonstrating a protective role of Prdx5 in ischemia-reperfusion injury in vivo. Adenoviral overexpression in rat liver transplantation model, proteomics (2D-PAGE/MALDI-TOF), Western blotting, immunohistochemistry, survival analysis Journal of hepatology Medium 20451279
2020 PRDX5 was identified as a novel binding partner of Nrf2 in NSCLC cells under H2O2-stimulated oxidative stress. The PRDX5–Nrf2 interaction promotes expression of NQO1 in NSCLC cells. Knockdown of both Nrf2 and PRDX5 significantly reduced tumor growth in animal models. Co-immunoprecipitation, Western blotting, shRNA knockdown, animal tumor growth assays Aging Medium 31899687
2020 ROS-induced hypomethylation of the PRDX5 promoter enhances STAT3 binding at two specific sites (−444 to −434 bp and −1417 to −1407 bp), increasing PRDX5 expression. STAT3 knockdown decreased PRDX5 protein levels while STAT3 overexpression increased them. PRDX5 overexpression activated the Nrf2 signaling pathway and promoted EMT (decreased E-cadherin, increased vimentin) in NSCLC cells under oxidative stress. Bisulfite sequencing PCR, ChIP assay, luciferase detection assay, STAT3 knockdown/overexpression, siRNA and pcDNA3.1 transfection with Western blotting International journal of molecular medicine Medium 33416106
2023 PRDX5 regulates the DNA damage response (DDR) through multiple mechanisms: (1) Plk1-mediated phosphorylation of ATM kinase triggering downstream Chek1/Chek2; (2) regulation of p53 acetylation at lysine 382 via Sirt2, which was identified as a novel deacetylase of p53 at K382 in a Prdx5-dependent manner; (3) induction of autophagy that recycles DDR molecules. Prdx5 knockdown induced γ-H2AX and 53BP1 (DNA damage markers), while exogenous Prdx5 decreased DNA damage and ATM activation in Pkd1 mutant renal epithelial cells. siRNA knockdown, γ-H2AX and 53BP1 immunofluorescence, Western blotting for phospho-ATM/Chek1/Chek2, p53 acetylation assays, autophagy assays, exogenous PRDX5 expression in Pkd1 mutant cells Human molecular genetics Medium 36067023
2023 PRDX5 promotes AR inhibitor resistance and castration-resistant prostate cancer (CRPC) development. The thioredoxin/peroxiredoxin pathway is upregulated in drug-tolerant persister (DTP) cells. Inhibition of PRDX5 suppresses DTP cell proliferation in culture and dampens CRPC development in animal models. Cell culture proliferation assays, animal models of CRPC, pathway analysis, PRDX5 inhibition Advanced science Medium 38115765
2023 PRDX5 and Nrf2 form a protein complex that is enhanced by oxidative stress (H2O2 treatment). The PRDX5–Nrf2 complex synergistically promotes NSCLC cell proliferation and drug resistance in zebrafish models. Co-immunoprecipitation, Western blotting, immunohistochemistry, zebrafish xenograft models Oncology research Medium 37305326
2025 During cryopreservation-induced oxidative stress in bull sperm, PRDX5 translocates intracellularly and forms high molecular weight oligomers that may shift from peroxidase to chaperone roles. PRDX5 interaction with TLR4 may be key to its intracellular transport. PRDX5 is also found in exosomal vesicles, suggesting a potential transport mechanism. Imaging Flow Cytometry, native PAGE and SDS-PAGE techniques (various), ROS/NO measurement, mitochondrial potential assay, DNA fragmentation assay Cell communication and signaling Low 39780184
2025 PRDX5 regulates mitochondrial function and myonuclear positioning during myogenesis. Prdx5-/- myotubes exhibit impaired nuclear spreading (clustered nuclei) and reduced mitochondrial ATP production. PRDX5 facilitates mitochondrial transport and nuclear positioning at least in part through transcriptional regulation of Rhot1 and Trak1 (key mitochondrial transport regulators). Double knockout of Prdx3 and Prdx5 accelerates muscle aging with increased mitochondrial H2O2 production, upregulating E3 ligases Atrogin1 and MuRF1. Prdx5-/- and Prdx3-/-;Prdx5-/- mouse models, confocal and super-resolution lattice SIM microscopy, Seahorse OCR assays, Rhot1/Trak1 knockdown, grip strength, treadmill performance, histology Journal of cachexia, sarcopenia and muscle High 41147088
2025 IER3 inhibits mitochondrial translocation of PRDX5 by interacting with the presenilin-associated rhomboid-like protease (Parl) and reducing its shear activity, thereby preventing cleavage and mitochondrial import of cytoplasmic PRDX5. Reduced mitochondrial PRDX5 impairs antioxidant capacity, causes oxidative mitochondrial damage and abnormal perinuclear mitochondrial clustering, promoting RTEC stress-induced senescence and AKI-to-CKD transition. IER3 knockout mice, RNA-seq, PRDX5 inhibition rescue experiments, co-immunoprecipitation (IER3–Parl interaction), mitochondrial fractionation, senescence assays Cellular and molecular life sciences Medium 41359162
2025 PRDX5 interacts with TFAM; PRDX5 overexpression enhances TFAM activation to counteract ROS-induced mitochondrial damage and restore mitochondrial homeostasis in renal tubular cells. TFAM knockdown reverses the mitochondrial functional improvements achieved through PRDX5 overexpression. Protein binding assays (PRDX5–TFAM interaction), ultrasound microbubble-mediated in situ PRDX5 overexpression, PRDX5 knockdown, TFAM knockdown, mtDNA leakage assay, mitochondrial function assays in CKD models Phytomedicine Low 39955823
2025 SIRT3 activates PRDX5 as its direct downstream effector in neurons; SIRT3 and PRDX5 co-localize in the anterior horn spinal cord neurons. Genetic silencing of PRDX5 partially attenuated SIRT3-mediated neuroprotection against apoptosis after spinal cord injury, placing PRDX5 downstream of SIRT3 in a neuroprotective axis. Transcriptome analysis of Sirt3-/- mice, SIRT3 agonist (honokiol) treatment, PRDX5 siRNA knockdown, immunofluorescence co-localization, neurological functional assessments in SCI mouse model Brain research bulletin Medium 40818507
2025 Prdx5 promotes M1 macrophage polarization and apoptosis of prostate epithelial cells via the TLR4/NF-κB signaling pathway in an ROS-dependent manner. Prdx5 silencing suppressed M1 polarization, reduced epithelial cell apoptosis, and mitigated experimental autoimmune prostatitis. Prdx5 expression in macrophages is regulated in an ROS-dependent manner. Prdx5 siRNA silencing, Western blotting, RT-qPCR, flow cytometry, cell co-culture, immunofluorescence staining, EAP mouse model International immunopharmacology Medium 40015209
2026 Acetylation of PRDX5 inhibits its antioxidant and anti-apoptotic functions. OGD/R increased PRDX5 acetylation in retinal neurons; NAM treatment that increased acetylation elevated ROS and apoptosis, while NRC treatment that reduced acetylation decreased ROS and apoptosis. Inhibiting deacetylation abolished the protective effect of PRDX5 overexpression, demonstrating that acetylation status directly controls PRDX5 activity. OGD/R model in R28 cells, aHIOP mouse model, nicotinamide and NRC pharmacological modulation of acetylation, PRDX5 knockdown and overexpression, ROS measurement, mitochondrial membrane potential, TUNEL/PI staining, LDH release Tissue & cell Medium 41740330
2025 Salvianolic acid B (SAB) binds directly to 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 abrogated SAB's protective effects on cisplatin-induced acute kidney injury. DARTS (drug affinity responsive target stability), CETSA (cellular thermal shift assay), molecular docking, PRDX5 siRNA knockdown, cisplatin- and folic acid-induced AKI models in vivo and in vitro FASEB journal Medium 40654183
2024 Stachyose (STA) inhibits PRDX5 enzyme activity and disrupts the PRDX5–NRF2 protein–protein interaction, leading to decreased NQO1 levels and accumulation of quinone radicals, ultimately inducing apoptosis of AR-inhibitor drug-tolerant persister cells and slowing CRPC progression. PRDX5 enzyme activity assay, PRDX5–NRF2 interaction disruption assay, NQO1 Western blotting, apoptosis assay, pharmacokinetic analysis in CRPC mouse model International journal of biological macromolecules Medium 39168191
2022 Porcine PRDX5 (pPRDX5) inhibits inflammatory responses induced by TNF-α or PRRSV in porcine alveolar macrophages. Knockdown of endogenous pPRDX5 enhanced inflammatory responses. The anti-inflammatory activity of pPRDX5 depends on its peroxidase activity, as shown by activity-dependent modulation experiments. Recombinant pPRDX5 protein treatment, siRNA knockdown of endogenous pPRDX5, TNF-α and PRRSV stimulation, inflammatory marker measurement, peroxidase activity assays Developmental and comparative immunology Medium 35985565

Source papers

Stage 0 corpus · 74 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci. Nature genetics 2036 21102463
2003 Structure, mechanism and regulation of peroxiredoxins. Trends in biochemical sciences 1912 12517450
2005 A human protein-protein interaction network: a resource for annotating the proteome. Cell 1704 16169070
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2009 Defining the human deubiquitinating enzyme interaction landscape. Cell 1282 19615732
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2010 Genome-wide association study in alopecia areata implicates both innate and adaptive immunity. Nature 621 20596022
2008 Large-scale proteomics and phosphoproteomics of urinary exosomes. Journal of the American Society of Nephrology : JASN 607 19056867
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
2000 Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. The Journal of biological chemistry 385 10751410
2020 Virus-Host Interactome and Proteomic Survey Reveal Potential Virulence Factors Influencing SARS-CoV-2 Pathogenesis. Med (New York, N.Y.) 291 32838362
2020 Phosphorylated tau interactome in the human Alzheimer's disease brain. Brain : a journal of neurology 290 32812023
2011 A function for cyclin D1 in DNA repair uncovered by protein interactome analyses in human cancers. Nature 269 21654808
2021 Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context. Cell metabolism 239 34800366
2009 Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). Journal of proteome research 237 19199708
1999 Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. The Journal of biological chemistry 209 10521424
2011 Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin. Antioxidants & redox signaling 208 20977338
2001 Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. Journal of molecular biology 196 11518528
2020 Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals spatially organized RAC1 signalling from integrin adhesions. Nature cell biology 194 32203420
2020 Synthetic Lethal and Resistance Interactions with BET Bromodomain Inhibitors in Triple-Negative Breast Cancer. Molecular cell 159 32416067
2019 A protein-interaction network of interferon-stimulated genes extends the innate immune system landscape. Nature immunology 159 30833792
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
2004 Human peroxiredoxin 5 is a peroxynitrite reductase. FEBS letters 155 15280035
2010 A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome. The EMBO journal 153 20186120
2000 Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis. Biochemical and biophysical research communications 144 10679306
2013 In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 138 23533145
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 29 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 18 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
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 Identification of PRDX5 as A Target for The Treatment of Castration-Resistant Prostate Cancer. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 12 38115765
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 8 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 PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress. Cell communication and signaling : CCS 4 39780184
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
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 3 39900986
2025 Prdx5 regulates macrophage polarization by modulating the TLR4/NF-κB pathway to promote apoptosis in chronic prostatitis. International immunopharmacology 3 40015209
2022 Molecular cloning, prokaryotic expression and the anti-inflammatory activity of porcine PRDX5. Developmental and comparative immunology 3 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 2 40122834
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 2 40654183
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
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 1 40798978
2025 Activation of SIRT3 / PRDX5 signaling inhibits apoptosis after acute spinal cord injury in mice. Brain research bulletin 1 40818507
2024 First report of Peroxiredoxin-5 (PRDX5) in starry flounder (Platichthys stellatus): Molecular features and expression analysis. Developmental and comparative immunology 1 39571926
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
2026 CD133+ Lung Cancer Stem-like Cells Resist Plasma-activated Medium Through PRDX5-mediated Antioxidant Defense. Anticancer research 0 41760234
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