Affinage

PARP3

Protein mono-ADP-ribosyltransferase PARP3 · UniProt Q9Y6F1

Length
533 aa
Mass
60.1 kDa
Annotated
2026-06-10
68 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PARP3 is a DNA damage-responsive mono(ADP-ribosyl)transferase that couples detection of ligatable DNA breaks to chromatin-based regulation of double-strand break (DSB) repair and gene silencing (PMID:27530147, PMID:29361132). Unlike poly-ADP-ribosylating family members, PARP3 catalyzes mono-ADP-ribosylation, auto-modifying itself and transferring ADP-ribose onto protein substrates, and it activates PARP1 in trans through its WGR domain (PMID:20064938). PARP3 is preferentially activated by breaks bearing a 5'-phosphate and by nicked mononucleosomes, on which it specifically mono-ribosylates histone H2B at Glu2, via an allosteric WGR-domain mechanism shared with PARP1/PARP2 (PMID:24928857, PMID:27530147). Strikingly, it can also mono-ADP-ribosylate DNA termini themselves at 5'/3'-phosphate residues, creating a primed substrate for PAR elongation by PARP1/PARP2 and for ligation by DNA ligases, defining a distinct break-repair route (PMID:29361132). In the DSB response, PARP3 acts together with APLF to accelerate nonhomologous end-joining and stabilize the XRCC4/DNA ligase IV complex on chromatin, and it interacts with and ADP-ribosylates Ku70/Ku80 to limit DNA end resection and govern the choice between NHEJ and homologous recombination (PMID:21211721, PMID:24598253). Through these activities PARP3 promotes long-range end joining, class switch recombination, chromosomal rearrangements, and control of G-quadruplex DNA levels (PMID:26000965, PMID:28447610, PMID:30213852). Beyond repair, PARP3 functions as a transcriptional regulator by cooperating with histone methyltransferases—recruiting G9a to establish H3K9me2 at repressed loci and recruiting/ADP-ribosylating Ezh2 to deposit H3K27me3 during myogenic differentiation (PMID:36109561, PMID:40248123). PARP3 also drives broader cellular programs: it promotes TGFβ/ROS-dependent epithelial-to-mesenchymal transition through a TG2-Snail-E-cadherin axis (PMID:27579892), sustains BRCA1-deficient tumor growth via ADP-ribosylation of GSK3β and Rictor/mTORC2 signaling (PMID:30442946), and drives macrophage inflammation through mono-ADP-ribosylation of cyclophilin A (Ppia) at Glu140 and downstream NF-κB activation (PMID:40461998).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2003 Medium

    Established the first cellular coordinates for PARP3 by mapping it to the daughter centriole and linking it to cell-cycle progression, raising the question of whether it is a structural centrosomal factor or an enzyme.

    Evidence Immunofluorescence, deletion-construct overexpression, and co-IP in human cells

    PMID:12640039

    Open questions at the time
    • Did not define catalytic activity or substrates
    • Centrosomal role mechanistically separate from later DNA-repair findings
  2. 2007 Medium

    Placed PARP3 simultaneously in Polycomb bodies and DNA-PKcs/Ku/ligase repair complexes, presaging its dual roles in gene silencing and DSB repair.

    Evidence Co-localization, reciprocal co-IP, and MS proteomics in human cells

    PMID:16924674

    Open questions at the time
    • Associations were correlative; no enzymatic role assigned
    • Substrates within these complexes unidentified
  3. 2010 High

    Resolved PARP3's enzymatic identity as a mono-ADP-ribosylase that, rather than being activated by DNA alone, activates PARP1 in trans through its WGR domain.

    Evidence In vitro ADP-ribosylation assays, co-IP, siRNA knockdown, survival assay

    PMID:20064938

    Open questions at the time
    • Physiological protein substrates beyond histone H1 not yet defined
    • In vivo relevance of PARP1 trans-activation unclear
  4. 2011 High

    Defined PARP3 as a DSB-responsive accelerator of NHEJ acting through APLF to retain XRCC4/DNA ligase IV, and linked it to mitotic spindle and telomere integrity via NuMA and tankyrase 1.

    Evidence In vitro DSB stimulation, genetic epistasis with Aplf-/- B cells, live-cell recruitment imaging, KO mouse models, co-IP

    PMID:21211721 PMID:21270334

    Open questions at the time
    • How PARP3 activity translates to APLF recruitment not fully resolved
    • Direct substrate at the break not yet identified
  5. 2013 Medium

    Connected PARP3 to ATM signaling by showing it is required for ATM-dependent APLF Ser116 phosphorylation needed for DSB repair, and delivered a selective inhibitor with a defined structural basis.

    Evidence Depletion/inhibition with phospho-specific detection and laser-damage recruitment; crystal structures and cross-PARP profiling

    PMID:23449221 PMID:23742272

    Open questions at the time
    • Mechanism by which PARP3 enables ATM-dependent phosphorylation unresolved
    • Whether the inhibitor's effects are purely catalytic remains open
  6. 2014 High

    Identified the substrate preference (5'-phosphorylated breaks) and the WGR-centered allosteric activation mechanism, and showed PARP3 ADP-ribosylates Ku70/Ku80 to restrain end resection and bias pathway choice.

    Evidence In vitro assays with defined DNA substrates, domain deletion, co-IP, YFP-Ku80 live imaging, end-resection assay

    PMID:24598253 PMID:24928857

    Open questions at the time
    • Functional consequence of Ku ADP-ribosylation at the residue level not mapped
    • Quantitative contribution to HR/NHEJ balance in vivo unclear
  7. 2015 High

    Demonstrated a physiological immunological role: Parp3 loss enhances class switch recombination and biases junctions toward alternative end joining without affecting somatic hypermutation.

    Evidence Parp3 knockout B cells, CSR/SHM assays, AID ChIP, junction sequencing

    PMID:26000965

    Open questions at the time
    • Catalytic requirement for the CSR phenotype not established
    • Direct substrate controlling AID occupancy unknown
  8. 2016 High

    Established the chromatin substrate of PARP3—nicked nucleosomes activate it to trans-ribosylate histone H2B at Glu2—and confirmed a conserved DNA-break-sensing interface driving single-strand break repair.

    Evidence 2D NMR, mononucleosome binding/activity assays, site-specific ribosylation mapping, DT40 loss-of-function SSB repair

    PMID:27530147

    Open questions at the time
    • Downstream readers of H2B-Glu2 mono-ADP-ribosylation unidentified
    • In vivo relevance of nucleosome substrate preference not tested
  9. 2017 Medium

    Expanded PARP3's genome-stability role to regulation of G-quadruplex DNA, with G4 accumulation in PARP3-null cells suppressing repair and creating synthetic lethality upon G4 stabilization.

    Evidence Translocation reporter screen, PARP3 KO, G4 immunofluorescence, chemical G4 stabilization, synthetic lethality assay

    PMID:28447610

    Open questions at the time
    • Direct biochemical link between PARP3 catalysis and G4 resolution missing
    • Whether effect is enzyme-dependent unclear
  10. 2018 High

    Revealed that PARP3 can mono-ADP-ribosylate DNA termini themselves, generating a primed, ligatable substrate that defines a novel break-repair pathway, and extended its substrate range to GSK3β in BRCA1-deficient tumor signaling and to long-range end joining.

    Evidence In vitro ADP-ribosylation/ligation/BER reconstitution; CRISPR KO with catalytic-mutant rescue and in vivo tumorigenicity; KO murine translocation assays

    PMID:29361132 PMID:29520010 PMID:30213852 PMID:30397881 PMID:30442946

    Open questions at the time
    • In vivo prevalence of DNA-ADP-ribosylation versus protein modification unknown
    • How GSK3β ADP-ribosylation feeds Rictor ubiquitination mechanistically unresolved
  11. 2016 Medium

    Connected PARP3 to a cell-state program by showing it transduces TGFβ/ROS signaling into a TG2-Snail-E-cadherin EMT axis and stem-like properties.

    Evidence siRNA/overexpression, TGFβ treatment, ROS measurement, EMT marker and tumor-sphere assays

    PMID:27579892

    Open questions at the time
    • Catalytic substrate within the EMT axis not identified
    • Mechanism of ROS sensing by PARP3 unknown
  12. 2022 Medium

    Established PARP3 as a transcriptional co-regulator that physically and functionally partners with G9a to deposit H3K9me2 and repress adhesion and hypoxia-responsive genes.

    Evidence Reciprocal co-IP, H3K9me2 ChIP, siRNA/CRISPR KO, drug-sensitivity assay in glioblastoma cells

    PMID:36109561

    Open questions at the time
    • Whether G9a is an ADP-ribosylation substrate not tested
    • Catalytic dependence of repression unresolved
  13. 2023 Low

    Provided physical evidence that PARP3 binding alters nucleosome geometry, hinting at a structural role in chromatin compaction.

    Evidence Atomic force microscopy of PARP3-nucleosome complexes

    PMID:37240388

    Open questions at the time
    • Single biophysical method with no functional follow-up
    • Catalytic versus binding contribution undefined
  14. 2025 Medium

    Extended PARP3 substrate biology to immunity and development: it mono-ADP-ribosylates cyclophilin A at Glu140 to drive NF-κB-dependent macrophage inflammation, and recruits/ADP-ribosylates Ezh2 to deposit H3K27me3 during skeletal muscle differentiation.

    Evidence Co-IP, site-directed mutagenesis, in vitro ADP-ribosylation, NF-κB readouts and murine ALI model; Parp3 KO mice, H3K27me3 ChIP-seq, Ezh2 ChIP, myogenic differentiation assays

    PMID:40248123 PMID:40461998

    Open questions at the time
    • In vivo causality of Ppia-E140 modification within intact inflammation not fully isolated
    • Whether Ezh2 ADP-ribosylation directly drives recruitment unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved which PARP3 substrate—protein versus DNA termini—predominates in vivo across repair, transcriptional silencing, and inflammatory contexts, and how a single enzyme's catalysis is partitioned among these roles.
  • No unified model linking substrate choice to biological outcome
  • Catalytic dependence not established for several phenotypes (G4 control, EMT, G9a repression)

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016740 transferase activity 7 GO:0140096 catalytic activity, acting on a protein 5 GO:0003677 DNA binding 3 GO:0042393 histone binding 2 GO:0140097 catalytic activity, acting on DNA 1
Localization
GO:0005815 microtubule organizing center 2 GO:0000228 nuclear chromosome 1 GO:0005634 nucleus 1
Pathway
R-HSA-73894 DNA Repair 4 R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 2 R-HSA-4839726 Chromatin organization 2 R-HSA-1266738 Developmental Biology 1
Partners
APLFEHMT2EZH2NUMA1PARP1TNKSXRCC5XRCC6
Complex memberships
Polycomb group bodiesXRCC4/DNA ligase IV complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 PARP3 localizes preferentially to the daughter centriole throughout the cell cycle; its N-terminal domain (54 amino acids) is responsible for centrosomal localization. Overexpression of PARP3 or its N-terminal domain does not influence centrosomal duplication but interferes with G1/S cell cycle progression. PARP-1 also resides in the centrosome and interacts with PARP3. Immunofluorescence/subcellular fractionation, overexpression of deletion constructs, co-immunoprecipitation, cell cycle analysis Journal of cell science Medium 12640039
2007 PARP3 is a nuclear protein that associates with Polycomb group (PcG) bodies and is part of PcG protein complexes. Both PARP3 isoforms are also found in complexes with DNA-PKcs, PARP-1, DNA ligase III, DNA ligase IV, Ku70, and Ku80, implicating PARP3 in DNA damage repair complexes. Co-localization by immunofluorescence, co-immunoprecipitation, proteomics/mass spectrometry Journal of cellular biochemistry Medium 16924674
2010 PARP3 is a mono-ADP-ribosylase (not a poly-ADP-ribosylase) that auto-ribosylates and ribosylates histone H1 in vitro. PARP3 is not activated by DNA binding alone but instead interacts with PARP1 via its WGR domain and activates PARP1 in the absence of DNA, resulting in PAR synthesis by PARP1. PARP3 depletion does not sensitize cells to camptothecin-induced single-strand breaks. In vitro ADP-ribosylation assay, co-immunoprecipitation, siRNA knockdown, cell survival assay The Journal of biological chemistry High 20064938
2011 PARP3 is stimulated by DNA double-strand breaks (DSBs) in vitro and functions in the same pathway as the PAR-binding protein APLF to accelerate chromosomal DSB repair by NHEJ. PARP3 promotes accumulation of APLF at DSBs; APLF in turn promotes retention of the XRCC4/DNA ligase IV complex in chromatin. Absence of APLF biases class switch recombination toward microhomology-mediated end-joining, circumvented by XRCC4/DNA ligase IV overexpression. In vitro DSB stimulation assay, genetic epistasis (siRNA depletion, Aplf-/- B cells), live-cell imaging of factor recruitment, overexpression rescue, class switch recombination assay Molecular cell High 21211721
2011 PARP3 plays a role in cellular response to DSBs in concert with PARP1, and is a critical player in mitotic spindle stabilization and telomere integrity. PARP3 associates with and regulates the mitotic components NuMA and tankyrase 1. Loss-of-function human and mouse models, biochemical studies (co-immunoprecipitation), mitotic spindle analysis Proceedings of the National Academy of Sciences of the United States of America Medium 21270334
2013 ATM-dependent phosphorylation of APLF at Ser116 following DNA damage is dependent on PARP3 levels and on the APLF PBZ (PAR-binding zinc finger) domains. PARP3 and ATM function in a common signaling pathway to facilitate APLF-Ser116 phosphorylation, which is required for efficient DSB repair and cell survival after IR. siRNA depletion, chemical inhibition, phospho-specific antibody detection, laser-induced damage recruitment assay, cell survival assay Nucleic acids research Medium 23449221
2013 Crystal structures of PARP3 with a selective inhibitor (targeting the nicotinamide binding site) reveal the molecular basis for inhibitor selectivity among PARP family members. The compound is active in cells, eliciting PARP3-specific effects at submicromolar concentration. Crystal structure determination, in vitro profiling against 12 PARP family members, cell-based assay ACS chemical biology High 23742272
2014 PARP2 and PARP3 are preferentially activated by DNA breaks harboring a 5' phosphate (5'P), indicating selective activation at structures competent for DNA ligation. Unlike PARP1, the N-terminal regions of PARP2 and PARP3 are not strictly required for DNA binding or activation; instead the WGR domain is the central regulatory domain. PARP1, PARP2, and PARP3 share an allosteric mechanism of DNA-dependent catalytic activation through local destabilization of the catalytic domain. In vitro biochemical assays with defined DNA substrates, domain deletion analysis, allosteric activation studies Nucleic acids research High 24928857
2014 PARP3 interacts with and PARylates Ku70/Ku80. PARP3 depletion impairs recruitment of Ku80 to laser-induced DNA damage sites and induces an imbalance between BRCA1 and 53BP1, thereby compromising accurate C-NHEJ and increasing DNA end resection. Together with Ku80, PARP3 limits DNA end resection and influences the choice between HR and NHEJ pathways. Co-immunoprecipitation, siRNA depletion, live-cell imaging of YFP-Ku80 recruitment, in vitro PARylation assay, end resection assay Nucleic acids research High 24598253
2015 Parp3 deficiency results in enhanced class switch recombination (CSR) while somatic hypermutation (SHM) remains unaffected. Mechanistically, this is due to increased occupancy of AID at the donor (Sμ) switch region and increased DNA damage at switch region junctions, with a bias toward alternative end joining. Parp3 knockout B cells, CSR and SHM assays, ChIP for AID occupancy, junction sequencing PLoS genetics High 26000965
2016 PARP3 preferentially binds and is activated by mononucleosomes containing nicked DNA. When activated by nicked mononucleosomes, PARP3 mono-ribosylates histone H2B specifically at Glu2 (trans-ribosylation), whereas nicks in naked DNA stimulate PARP3 autoribosylation. PARP3 accelerates repair of chromosomal single-strand breaks in DT40 cells and uses a conserved DNA-binding interface to detect DNA breaks. 2D NMR, mononucleosome binding and activity assays, site-specific ribosylation mapping, DT40 cell loss-of-function SSB repair assay Nature communications High 27530147
2016 PARP3 plays an integral role in TGFβ- and ROS-dependent epithelial-to-mesenchymal transition (EMT). PARP3 depletion prevents the induction of a TG2-Snail-E-cadherin axis and inhibits TGFβ-induced EMT. PARP3 responds to TGFβ-induced ROS to promote this axis. PARP3 also promotes stem-like cell properties (SOX2, OCT4 expression; CD44high/CD24low population; tumor spheroid formation). siRNA depletion, overexpression, TGFβ treatment, ROS measurement, EMT marker analysis, tumor sphere formation assay Oncotarget Medium 27579892
2017 PARP3 promotes chromosomal rearrangements and regulates G quadruplex (G4) DNA in response to DNA damage. Loss of PARP3 leads to increased G4 DNA, which suppresses repair by both NHEJ and HR. Chemical stabilization of G4 DNA in PARP3-/- cells causes widespread DSBs and synthetic lethality. Zinc-finger nuclease translocation reporter screen, PARP3 knockout, G4 DNA immunofluorescence, chemical G4 stabilization, synthetic lethality assay Nature communications Medium 28447610
2018 PARP3 can mono(ADP-ribosyl)ate DNA itself—specifically 5'- and 3'-terminal phosphate residues at double- and single-strand break termini. PARP3-catalyzed DNA MARylation can serve as a primed substrate for further PAR chain elongation by PARP1/PARP2 and can be ligated to double-stranded DNA by DNA ligases. In vitro ADP-ribosylation assay with defined DNA substrates, ligation assay, cell-free extract PAR elongation assay Nucleic acids research High 29361132
2018 PARP3 ADP-ribosylates DNA (mono-ADP-ribosylation of gapped DNA), and the modified DNA can be ligated by DNA ligases and serve as a primed substrate for PAR elongation. This suggests a DNA break repair pathway involving PARP3-dependent DNA ADP-ribosylation followed by ligation and BER enzyme-mediated repair of ribo-AP sites. In vitro DNA ADP-ribosylation assay, ligation assay, BER reconstitution with purified proteins Scientific reports Medium 29520010
2018 PARP3 absence selectively suppresses growth and in vivo tumorigenicity of BRCA1-deficient TNBC cells via altered Rictor/mTORC2 signaling resulting from enhanced ubiquitination of Rictor. PARP3 interacts with and ADP-ribosylates GSK3β, a positive regulator of Rictor ubiquitination and degradation. Catalytic mutant PARP3 fails to rescue these phenotypes, demonstrating requirement for catalytic activity. CRISPR/nCas9 KO, co-immunoprecipitation, in vitro ADP-ribosylation assay, ubiquitination assay, in vivo tumorigenicity assay, catalytic mutant rescue Cell death and differentiation High 30442946
2018 Parp3 promotes long-range end joining and chromosomal rearrangements (translocations, class-switch recombination, inversions) in murine cells. In Parp3-deficient cells, translocation junctions have shorter deletion lengths, consistent with a role for Parp3 in DSB processing. Parp3 knockout murine embryonic stem cells, primary B cells, tail fibroblasts; translocation reporter assay, class-switch recombination assay, next-generation sequencing of junction sequences Proceedings of the National Academy of Sciences of the United States of America Medium 30213852
2018 PARP3-dependent mono(ADP-ribosyl)ation of DNA breaks can be followed by ligation and BER enzyme-mediated repair of ribo-AP sites, defining a new DNA break repair pathway involving PARP3 and BER components. In vitro reconstitution with purified PARP3 and BER proteins, DNA ligation assay Doklady. Biochemistry and biophysics Low 30397881
2022 PARP3 physically and functionally interacts with the histone H3K9 methyltransferase G9a to regulate G9a-dependent repression of adhesion genes (Nfasc, Parvb) and hypoxia-responsive genes (Hif-2α, Runx3, Mlh1, Ndrg1-4) in glioblastoma cells. PARP3/G9a cooperate for establishment of the repressive mark H3K9me2 at specific loci. Absence of PARP3 increases sensitivity of glioblastoma cells to microtubule-destabilizing agents. Co-immunoprecipitation, ChIP for H3K9me2, siRNA/CRISPR KO, gene expression analysis, drug sensitivity assay Scientific reports Medium 36109561
2023 PARP3 significantly alters the geometry of nucleosomes as measured by atomic force microscopy, suggesting a role for PARP3 in chromatin compaction regulation through direct binding to nucleosomes. Atomic force microscopy of PARP3-nucleosome complexes, geometric parameter measurement International journal of molecular sciences Low 37240388
2025 PARP3 promotes macrophage inflammation via mono-ADP-ribosylation of cyclophilin A (Ppia) at Glu140, leading to NF-κB activation and inflammatory cytokine production. PARP3 interacts with Ppia (confirmed by co-immunoprecipitation), and mutation of Ppia-E140 inhibits mono-ADP-ribosylation, Ppia secretion, and inflammatory response. The PARP3-specific inhibitor ME0328 blocks NF-κB pathway activation in macrophages and alleviates lung inflammation in a murine ALI model. Co-immunoprecipitation, in vitro mono-ADP-ribosylation assay, site-directed mutagenesis of Ppia-E140, siRNA knockdown, NF-κB pathway analysis, murine ALI model with ME0328 inhibitor Molecular medicine (Cambridge, Mass.) Medium 40461998
2025 Parp3 promotes enrichment of the repressive histone mark H3K27me3 at selected gene loci during skeletal muscle differentiation. Parp3 helps recruit Ezh2 (the H3K27me3 methyltransferase) to specific genes and ADP-ribosylates Ezh2 in vitro. Parp3-deficient mice show impaired skeletal muscle integrity and defective myogenic differentiation. Parp3 knockout mouse model, ChIP-seq for H3K27me3, Ezh2 ChIP, in vitro ADP-ribosylation of Ezh2, myogenic differentiation assay iScience Medium 40248123

Source papers

Stage 0 corpus · 68 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Expression of the IRT1 metal transporter is controlled by metals at the levels of transcript and protein accumulation. The Plant cell 466 12084831
2011 Monoubiquitin-dependent endocytosis of the iron-regulated transporter 1 (IRT1) transporter controls iron uptake in plants. Proceedings of the National Academy of Sciences of the United States of America 357 21628566
2011 PARP-3 and APLF function together to accelerate nonhomologous end-joining. Molecular cell 266 21211721
2014 Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1, PARP2 and PARP3. Experimental cell research 249 25017100
2018 Metal Sensing by the IRT1 Transporter-Receptor Orchestrates Its Own Degradation and Plant Metal Nutrition. Molecular cell 233 29547723
2014 PARP-2 and PARP-3 are selectively activated by 5' phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1. Nucleic acids research 232 24928857
2011 Poly(ADP-ribose) polymerase 3 (PARP3), a newcomer in cellular response to DNA damage and mitotic progression. Proceedings of the National Academy of Sciences of the United States of America 232 21270334
2014 Polarization of IRON-REGULATED TRANSPORTER 1 (IRT1) to the plant-soil interface plays crucial role in metal homeostasis. Proceedings of the National Academy of Sciences of the United States of America 211 24843126
2010 PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNA. The Journal of biological chemistry 130 20064938
2003 PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. Journal of cell science 125 12640039
1994 Nucleotide sequences of the genes coding for the TEM-like beta-lactamases IRT-1 and IRT-2 (formerly called TRI-1 and TRI-2). FEMS microbiology letters 113 8056297
2018 Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation. Nucleic acids research 106 29361132
2021 PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling. International journal of molecular sciences 99 34066057
2007 PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery. Journal of cellular biochemistry 98 16924674
2014 PARP3 affects the relative contribution of homologous recombination and nonhomologous end-joining pathways. Nucleic acids research 88 24598253
2016 PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2B(Glu2). Nature communications 74 27530147
2016 PARP3 controls TGFβ and ROS driven epithelial-to-mesenchymal transition and stemness by stimulating a TG2-Snail-E-cadherin axis. Oncotarget 71 27579892
2016 The PARP Inhibitor AZD2461 Provides Insights into the Role of PARP3 Inhibition for Both Synthetic Lethality and Tolerability with Chemotherapy in Preclinical Models. Cancer research 69 27550455
2018 Inoculation with Bacillus subtilis and Azospirillum brasilense Produces Abscisic Acid That Reduces Irt1-Mediated Cadmium Uptake of Roots. Journal of agricultural and food chemistry 65 29738246
2018 Dna is a New Target of Parp3. Scientific reports 62 29520010
2013 The PARP3- and ATM-dependent phosphorylation of APLF facilitates DNA double-strand break repair. Nucleic acids research 54 23449221
2013 PARP inhibitor with selectivity toward ADP-ribosyltransferase ARTD3/PARP3. ACS chemical biology 49 23742272
1999 Isolation and characterization of human and mouse ZIRTL, a member of the IRT1 family of transporters, mapping within the epidermal differentiation complex. Genomics 48 10610721
2019 The bifunctional transporter-receptor IRT1 at the heart of metal sensing and signalling. The New phytologist 43 30929276
2017 PARP3 is a promoter of chromosomal rearrangements and limits G4 DNA. Nature communications 35 28447610
2018 PARP3, a new therapeutic target to alter Rictor/mTORC2 signaling and tumor progression in BRCA1-associated cancers. Cell death and differentiation 32 30442946
2020 Melatonin alleviates cadmium toxicity by reducing nitric oxide accumulation and IRT1 expression in Chinese cabbage seedlings. Environmental science and pollution research international 28 33236311
2019 PARP3 comes to light as a prime target in cancer therapy. Cell cycle (Georgetown, Tex.) 27 31095444
2009 A new cystic fibrosis newborn screening algorithm: IRT/IRT1 upward arrow/DNA. The Journal of pediatrics 26 19540513
2018 PARP3 inhibitors ME0328 and olaparib potentiate vinorelbine sensitization in breast cancer cell lines. Breast cancer research and treatment 25 30039287
2022 Differential metal sensing and metal-dependent degradation of the broad spectrum root metal transporter IRT1. The Plant journal : for cell and molecular biology 24 36269689
2011 NFAT regulates the expression of AIF-1 and IRT-1: yin and yang splice variants of neointima formation and atherosclerosis. Cardiovascular research 24 22116621
2023 Ferrous iron uptake via IRT1/ZIP evolved at least twice in green plants. The New phytologist 23 36626937
2020 Different regulation of PARP1, PARP2, PARP3 and TRPM2 genes expression in acute myeloid leukemia cells. BMC cancer 22 32423430
2020 Enhanced Cadmium Accumulation and Tolerance in Transgenic Hairy Roots of Solanum nigrum L. Expressing Iron-Regulated Transporter Gene IRT1. Life (Basel, Switzerland) 21 33287205
2015 Parp3 negatively regulates immunoglobulin class switch recombination. PLoS genetics 18 26000965
2014 Poly (ADP-ribose) polymerase 3 (PARP3), a potential repressor of telomerase activity. Journal of experimental & clinical cancer research : CR 16 24528514
1998 IRT-1, a novel interferon-gamma-responsive transcript encoding a growth-suppressing basic leucine zipper protein. The Journal of biological chemistry 16 9614071
2020 Impact of PARP1, PARP2 & PARP3 on the Base Excision Repair of Nucleosomal DNA. Advances in experimental medicine and biology 15 32383115
2013 The extracellular loop of IRT1 ZIP protein--the chosen one for zinc? Journal of inorganic biochemistry 15 23706761
2016 Transcription of the mating-type-regulated lncRNA IRT1 is governed by TORC1 and PKA. Current genetics 14 27520925
2002 Cloning and expression of PARP-3 (Adprt3) and U3-55k, two genes closely linked on mouse chromosome 9. Folia biologica 13 12448766
2022 PARP3 supervises G9a-mediated repression of adhesion and hypoxia-responsive genes in glioblastoma cells. Scientific reports 12 36109561
2015 PARP3 interacts with FoxM1 to confer glioblastoma cell radioresistance. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 12 26040766
2014 An uncleaved signal peptide directs the Malus xiaojinensis iron transporter protein Mx IRT1 into the ER for the PM secretory pathway. International journal of molecular sciences 12 25387073
2020 Combination of Selective PARP3 and PARP16 Inhibitory Analogues of Latonduine A Corrects F508del-CFTR Trafficking. ACS omega 11 33073085
2019 Design, Synthesis and Molecular Modeling Study of Conjugates of ADP and Morpholino Nucleosides as A Novel Class of Inhibitors of PARP-1, PARP-2 and PARP-3. International journal of molecular sciences 11 31892271
2018 Parp3 promotes long-range end joining in murine cells. Proceedings of the National Academy of Sciences of the United States of America 11 30213852
2011 Immunolocalization of H(+)-ATPase and IRT1 enzymes in N(2)-fixing common bean nodules subjected to iron deficiency. Journal of plant physiology 11 22078996
2009 Assessment of PARP-3 distribution in tissues of cynomolgous monkeys. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 11 19332431
2023 Mitigating cadmium accumulation in dicotyledonous vegetables by iron fertilizer through inhibiting Fe transporter IRT1-mediated Cd uptake. Chemosphere 10 37898465
2015 Expression of Malus xiaojinensis IRT1 (MxIRT1) protein in transgenic yeast cells leads to degradation through autophagy in the presence of excessive iron. Yeast (Chichester, England) 10 25871543
2018 The Development of a Biotinylated NAD+-Applied Human Poly(ADP-Ribose) Polymerase 3 (PARP3) Enzymatic Assay. SLAS discovery : advancing life sciences R & D 7 29676938
2023 Establishment of hairy root system of transgenic IRT1 brassica campestris L. and preliminary study of its effect on cadmium enrichment. International journal of phytoremediation 6 36597829
2022 The role of iron nanoparticles on morpho-physiological traits and genes expression (IRT1 and CAT) in rue (Ruta graveolens). Plant molecular biology 6 35793007
2018 A New DNA Break Repair Pathway Involving PARP3 and Base Excision Repair Proteins. Doklady. Biochemistry and biophysics 6 30397881
2024 Enhancing cisplatin drug sensitivity through PARP3 inhibition: The influence on PDGF and G-coupled signal pathways in cancer. Chemico-biological interactions 4 38830565
2023 PARP3 Affects Nucleosome Compaction Regulation. International journal of molecular sciences 4 37240388
2025 PARP3 promotes macrophage inflammation via mono ADP ribosylation of Ppia Glu140. Molecular medicine (Cambridge, Mass.) 3 40461998
2025 Canonical tyrosine-based motifs are required for constitutive endocytosis and polarity of IRT1 and contribute to metal uptake. The Plant journal : for cell and molecular biology 3 41075308
2025 Parp3 assists muscle function and skeletal muscle differentiation by selectively adjusting H3K27me3 enrichment. iScience 2 40248123
2023 Fall of PARP3 restrains Lgr5+ intestinal stem cells proliferation and mucosal renovation in intestinal aging. Mechanisms of ageing and development 2 36870456
2017 Corrigendum: PARP3 is a promoter of chromosomal rearrangements and limits G4 DNA. Nature communications 2 28607496
2017 Purification of Recombinant Human PARP-3. Methods in molecular biology (Clifton, N.J.) 2 28695522
2025 PARP3 Promotes AML Progression via Activation of PI3K/AKT/mTOR Signaling. Cancers 1 41008918
2026 Iron status modulates cadmium tolerance: mechanistic insights from MsbHLH60-mediated regulation of the FIT/IRT1 module in alfalfa. Frontiers in plant science 0 42179482
2023 Purification of Recombinant Human PARP-3. Methods in molecular biology (Clifton, N.J.) 0 36515851
2020 Development of mutant human immunoreactive trypsinogen 1 (IRT1) and mutant human immunoreactive trypsinogen 2 (IRT2) for use in immunoassays. Protein expression and purification 0 31972264

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