Affinage

PARP12

Protein mono-ADP-ribosyltransferase PARP12 · UniProt Q9H0J9

Length
701 aa
Mass
79.1 kDa
Annotated
2026-06-10
40 papers in source corpus 16 papers cited in narrative 15 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/6 claims corpus-supported (83%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PARP12 is an interferon-stimulated mono-ADP-ribosyltransferase that couples nuclear and cytoplasmic stress sensing to the control of membrane traffic, mRNA translation, and innate antiviral defense (PMID:25086041, PMID:29070863). At the trans-Golgi network its catalytic activity is switched on by direct phosphorylation from protein kinase D, where it mono-ADP-ribosylates Golgin-97 on an acidic cluster to drive the formation and fission of carriers delivering basolateral cargoes such as E-cadherin and VSVG to the plasma membrane (PMID:34969853). Upon stress, nuclear PARP1 activation generates poly-ADP-ribose that binds the PARP12 WWE domain, triggering reversible translocation from the Golgi to stress granules; this departure disassembles the Golgi, blocks anterograde traffic, and—via its N-terminal CCCH Zn-finger RNA-binding domain together with an intact catalytic domain—suppresses mRNA translation (PMID:25086041, PMID:29070863). As an antiviral effector, PARP12 ADP-ribosylates the viral nonstructural proteins NS1 and NS3 to trigger their proteasomal degradation and restrict Zika virus, an activity potentiated by its partner PARP11 (PMID:29921658, PMID:34187568), and it restricts coronavirus replication in mice through ADP-ribosyltransferase activity opposed by the viral Mac1 macrodomain (PMID:37695054, PMID:37398292). PARP12 also MARylates signaling and survival regulators: it modifies RIPK1 and RIPK3 downstream of IFNγ/TNFα to promote necroptosis while suppressing apoptosis (PMID:40489618), and modifies AKT to sustain its activation in breast cancer cells (PMID:39847113). Independent of catalysis, PARP12 stabilizes FHL2 against proteasomal degradation to restrain TGF-β1-driven epithelial-mesenchymal transition (PMID:30154409), and it engages ISG15 to promote MFN1/2 ISGylation and limit mitophagy (PMID:39465252).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2014 Medium

    Established PARP12 as an interferon-stimulated gene whose subcellular targeting dictates function, linking its RNA-binding and catalytic domains to translational arrest at stress granules.

    Evidence Ectopic expression, stress granule co-localization, deletion mutagenesis, translational reporters and NF-κB assays in cells

    PMID:25086041

    Open questions at the time
    • Direct RNA or protein substrates of the translational block not identified
    • Reconstitution of the catalytic requirement not performed
    • Mechanism linking p62/SQSTM1 association to NF-κB not resolved
  2. 2017 High

    Defined the trigger for PARP12 relocalization: nuclear PARP1-generated PAR binds the WWE domain to drive Golgi-to-stress-granule translocation, coupling nuclear stress to a reversible Golgi/traffic block.

    Evidence Live-cell imaging, PARP1 modulation, WWE PAR-binding assay, Golgi morphology and anterograde traffic assays with wash-out rescue

    PMID:29070863

    Open questions at the time
    • Golgi substrates mediating traffic block not yet identified at this stage
    • Structural basis of WWE-PAR recognition not resolved
  3. 2018 High

    Demonstrated a direct antiviral catalytic mechanism: PARP12 ADP-ribosylates Zika NS1 and NS3 to trigger their proteasomal degradation and restrict viral replication.

    Evidence CRISPR ISG knockout screen, A549 KO, NS1/NS3 western blot, proteasome inhibitor rescue and ADP-ribosylation assay

    PMID:29921658

    Open questions at the time
    • Modified residues on NS1/NS3 not mapped
    • E3 ligase coupling MARylation to degradation unknown
  4. 2018 Medium

    Revealed a catalysis-independent role: PARP12 binds and stabilizes FHL2 against ubiquitin-mediated degradation to restrain TGF-β1-driven EMT and tumor invasion.

    Evidence Affinity purification, reciprocal co-IP, ubiquitination assay, negative in vitro ADP-ribosylation of FHL2, siRNA and in vivo metastasis model

    PMID:30154409

    Open questions at the time
    • Mechanism by which PARP12 shields FHL2 from ubiquitination unknown
    • Single lab; reciprocal validation in independent systems lacking
  5. 2021 Medium

    Identified PARP11 as a physical partner that potentiates PARP12-mediated ADP-ribosylation and degradation of Zika NS1/NS3, defining cooperative anti-viral PARP activity.

    Evidence Single and double KO HEK293T lines, co-IP, NS1/NS3 western blot, immunofluorescence

    PMID:34187568

    Open questions at the time
    • Whether PARP11 modifies PARP12 or co-modifies substrates unresolved
    • Structural basis of the interaction unknown
  6. 2022 High

    Pinpointed Golgin-97 as the TGN substrate and PKD as the upstream activating kinase, mechanistically explaining how PARP12 controls basolateral cargo carrier formation.

    Evidence In vitro ADP-ribosylation with site-directed mutagenesis, PARP12 depletion, cargo transport and Rab11 colocalization assays, PKD kinase assay and inhibition

    PMID:34969853

    Open questions at the time
    • Reader of ADP-ribosylated Golgin-97 driving fission not identified
    • Generality across other cargoes beyond E-cadherin/VSVG not defined
  7. 2022 Low

    Reported a mitochondrial localization and a role supporting UCP1 expression and respiration in thermogenic adipocytes.

    Evidence qRT-PCR, western blot, fractionation/immunofluorescence, siRNA and overexpression, Seahorse respiration assay

    PMID:35916471

    Open questions at the time
    • No molecular mechanism connecting PARP12 to UCP1 or respiration identified
    • Mitochondrial localization not functionally dissected
    • Single lab, not independently confirmed
  8. 2023 High

    Extended antiviral function to coronaviruses in vivo, showing PARP12 is a genetically required restriction factor whose ADP-ribosyltransferase activity is counteracted by the viral Mac1 macrodomain.

    Evidence PARP12-/- mice, BMDM siRNA screen, viral replication and liver pathology assays, lethality study

    PMID:37398292 PMID:37695054

    Open questions at the time
    • Coronavirus substrates of PARP12 not defined
    • Cell types responsible for in vivo restriction not delineated
  9. 2023 Medium

    Uncovered a meiotic role: PARP12 localizes near spindle poles and is required for spindle integrity, chromosome alignment, and asymmetric division in mouse oocytes.

    Evidence Immunofluorescence across meiotic stages, knockdown, spindle/chromosome/aneuploidy scoring, BubR1 and F-actin staining

    PMID:37305966

    Open questions at the time
    • Spindle/actin substrates of PARP12 not identified
    • Whether catalytic activity is required not tested
  10. 2024 Medium

    Connected PARP12 to PTM cross-talk and transcriptional control: it engages ISG15 to drive MFN1/2 ISGylation, limiting mitophagy, and is transcriptionally induced by IRF1.

    Evidence Mass spectrometry, co-IP, ISGylation/ubiquitination/SUMOylation assays, ChIP of IRF1 on PARP12 promoter, PINK1/Parkin analysis, rat OA model

    PMID:39465252

    Open questions at the time
    • Whether PARP12 catalysis is required for ISG15 effect unclear
    • Direct MFN1/2 modification by PARP12 not established
  11. 2025 High

    Defined PARP12 as a regulator of cell-death fate, MARylating RIPK1/RIPK3 to promote necroptosis and suppress apoptosis downstream of IFNγ/TNFα with in vivo antiviral consequences.

    Evidence In vitro MARylation assay mapping RIPK1 domains, RIPK kinase assays, PARP12-/- cells and mice, necroptosis/apoptosis assays, influenza A model

    PMID:40489618

    Open questions at the time
    • Modified RIPK1/RIPK3 residues not pinpointed
    • Reader/eraser of these marks unknown
  12. 2025 Medium

    Identified AKT as a substrate, with PARP12 MARylation required for AKT activation and survival signaling in ER-positive breast cancer cells.

    Evidence ADP-ribosylation assay with AKT, siRNA, AKT activity and downstream p53/FOXO1 readouts, p53-AKT co-IP, apoptosis assay

    PMID:39847113

    Open questions at the time
    • AKT modification site not mapped
    • Single lab; in vivo relevance not tested
  13. 2025 Medium

    Extended ADP-ribosylation to RNA itself: PARP12 modifies chikungunya and cellular mRNAs (including insulin mRNA) to block translation, alter localization, accelerate decay, and trigger antiviral gene expression.

    Evidence RNA ribosylation assays, cell-free and infected-cell translation assays, viral RNA decay, antiviral gene expression, RNA localization in MIN6 cells (preprints)

    PMID:40470236 PMID:bio_10.1101_2025.07.18.665567

    Open questions at the time
    • Preprint, not peer-reviewed
    • Chemistry/site of RNA modification not fully defined
    • Mechanism linking RNA mark to decay/localization unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How PARP12's distinct localization-defined activities (TGN traffic, stress-granule translation arrest, mitochondrial/spindle roles, cell-death control) are integrated and selectively engaged remains unresolved.
  • No unifying model for substrate selection across compartments
  • Readers/erasers of PARP12-deposited marks largely unknown
  • Relative contribution of catalytic vs scaffolding functions unclear

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 4 GO:0003723 RNA binding 3 GO:0016740 transferase activity 3 GO:0140098 catalytic activity, acting on RNA 2
Localization
GO:0005794 Golgi apparatus 2 GO:0005829 cytosol 2
Pathway
R-HSA-168256 Immune System 3 R-HSA-5357801 Programmed Cell Death 2 R-HSA-8953854 Metabolism of RNA 2 R-HSA-9609507 Protein localization 2
Partners
AKTFHL2GOLGIN-97ISG15PARP11RIPK1RIPK3

Evidence

Reading pass · 15 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2014 PARP12 is an interferon-stimulated gene (ISG) that localizes to stress granules upon ectopic expression or oxidative stress, where it blocks mRNA translation. Both the N-terminal RNA-binding domain (five CCCH-type Zn-fingers) and an intact catalytic domain are required for translational suppression. Upon LPS stimulation, PARP12 instead localizes to p62/SQSTM1-containing structures, and deletion of the N-terminal domain promotes this association, correlating with increased NF-κB signaling. Ectopic expression, stress granule co-localization, deletion mutagenesis, translational reporter assays, co-immunoprecipitation with p62/SQSTM1, NF-κB reporter assay The Journal of biological chemistry Medium 25086041
2017 PARP12 is a Golgi-localized mono-ADP-ribosyltransferase that reversibly translocates from the trans-Golgi network to stress granules under stress. PARP1 activation in the nucleus produces poly-ADP-ribose (PAR) polymers that directly bind the PARP12 WWE domain, driving this translocation. PARP12 departure from the Golgi causes Golgi membrane disassembly and a block in anterograde membrane traffic, which is reversible upon stress removal. Live-cell imaging, PARP1 inhibition/activation, PAR-binding assay via WWE domain, Golgi morphology analysis, anterograde traffic assay, drug wash-out rescue experiment Scientific reports High 29070863
2018 PARP12 restricts Zika virus replication by mediating ADP-ribosylation of the viral nonstructural proteins NS1 and NS3, which triggers their proteasome-dependent degradation. Knockout of PARP12 in A549 cells enhanced Zika virus replication. CRISPR knockout screen (21 ISGs), individual ISG knockout in A549 cells, western blot for NS1/NS3 protein levels, proteasome inhibitor rescue experiment, ADP-ribosylation assay Science signaling High 29921658
2018 PARP12 interacts with four-and-a-half LIM-only protein 2 (FHL2) via protein affinity purification. PARP12 stabilizes FHL2 protein by protecting it from ubiquitin-mediated proteasomal degradation, and this stabilization is independent of PARP12 enzymatic activity. PARP12 deficiency increases TGF-β1 expression and promotes epithelial-mesenchymal transition, increasing migration and invasion of hepatocellular carcinoma cells. Protein affinity purification, co-immunoprecipitation, ubiquitination assay, in vitro ADP-ribosylation assay (negative for FHL2), siRNA knockdown, in vivo metastasis model Cell death & disease Medium 30154409
2021 PARP11 physically interacts with PARP12 (confirmed by co-immunoprecipitation) and promotes PARP12-mediated ADP-ribosylation and proteasomal degradation of Zika virus NS1 and NS3 proteins. In PARP11/PARP12 double-knockout cells, NS1/NS3 degradation is further impaired relative to single knockouts, demonstrating synergistic anti-Zika activity. PARP11/PARP12 single and double knockout HEK293T lines, co-immunoprecipitation, western blot for NS1/NS3 levels, immunofluorescence Cell & bioscience Medium 34187568
2022 PARP12 mono-ADP-ribosylates Golgin-97 at an acidic cluster in its coiled-coil domain at the trans-Golgi network. This modification is required for the formation and fission of carriers transporting specific basolateral cargoes (E-cadherin and VSVG). PARP12 depletion or mutation of the Golgin-97 modification site causes accumulation of these cargoes in a trans-Golgi/Rab11-positive intermediate compartment, delaying their transport to the plasma membrane. PARP12 enzymatic activity depends on its direct phosphorylation by protein kinase D (PKD) at the TGN. In vitro ADP-ribosylation assay, site-directed mutagenesis of Golgin-97 acidic cluster, PARP12 depletion (siRNA/KO), cargo transport assay (E-cadherin, VSVG, TNFα), Rab11 colocalization, PKD kinase assay, PKD inhibition, phosphorylation mapping Proceedings of the National Academy of Sciences of the United States of America High 34969853
2023 PARP12 knockout in mice increases replication of a coronavirus (MHV) Mac1 mutant in bone-marrow-derived macrophages and in vivo, and worsens liver pathology in A59-infected mice. This establishes PARP12 as a required innate immune restriction factor against coronavirus infection in cell culture and in animals, acting via its ADP-ribosyltransferase activity that is counteracted by the viral Mac1 macrodomain. PARP12-/- mouse generation, siRNA screen in BMDMs, viral replication assay, liver pathology assessment, lethality study Journal of virology High 37398292 37695054
2023 PARP12 localizes near spindle poles during meiotic metaphase I and II in mouse oocytes. PARP12 depletion causes spindle disorganization, chromosome misalignment, aneuploidy, spindle assembly checkpoint activation (BubR1 signal), and reduction of F-actin in metaphase I oocytes, demonstrating a required role in meiotic spindle integrity and asymmetric division. Immunofluorescence (localization at GV, MI, MII), morpholino/siRNA knockdown, spindle morphology analysis, chromosome spread and aneuploidy scoring, BubR1 immunostaining, F-actin staining, transcriptomic analysis Journal of cellular physiology Medium 37305966
2022 PARP12 is highly expressed in brown adipose tissue and localizes primarily to mitochondria. Knockdown of PARP12 reduces UCP1 expression and decreases mitochondrial respiration in thermogenic adipocytes, while overexpression reverses these effects. qRT-PCR, western blot, subcellular fractionation/immunofluorescence (mitochondrial localization), siRNA knockdown and overexpression, mitochondrial oxygen consumption assay (Seahorse) Adipocyte Low 35916471
2024 PARP12 interacts with ISG15 (identified by mass spectrometry and co-immunoprecipitation) and upregulates ISGylation of mitofusin 1 and 2 (MFN1/2), which decreases MFN1/2 ubiquitination and SUMOylation, thereby inhibiting PINK1/Parkin-dependent mitophagy in chondrocytes. IRF1, activated by inflammatory cytokines, directly binds the PARP12 promoter to drive PARP12 transcription. Mass spectrometry, co-immunoprecipitation, ISGylation assay, ubiquitination assay, SUMOylation assay, ChIP (IRF1-PARP12 promoter), PINK1/Parkin pathway analysis, rat OA model Bone research Medium 39465252
2025 PARP12 catalyzes mono-ADP-ribosylation (MARylation) of RIPK1 (in both its intermediate domain and kinase domain) and RIPK3 in cells stimulated by IFNγ and TNFα. PARP12-mediated MARylation of RIPK1 promotes RIPK1 kinase activation and its interaction with RIPK3 to promote necroptosis, while inhibiting RIPK1–caspase-8 binding to suppress apoptosis. PARP12 deficiency reduces necroptosis, sensitizes cells to apoptosis, and also promotes expression of a subset of ISGs, conferring protection against influenza A virus lethality in mice. Co-immunoprecipitation, in vitro MARylation assay, RIPK1/RIPK3 kinase activity assay, PARP12-/- cells and mice, necroptosis/apoptosis assays, influenza A virus infection model Proceedings of the National Academy of Sciences of the United States of America High 40489618
2025 PARP12 mono-ADP-ribosylates AKT, which is required for AKT activation in oestrogen receptor-positive breast cancer cells. Transcriptional inhibition of PARP12 reduces AKT activity, increases DNA damage, augments p53 nuclear localization, promotes p53–AKT interaction, and increases FOXO1 protein levels leading to apoptotic cell death. ADP-ribosylation assay (AKT as substrate), PARP12 siRNA knockdown, AKT activity assay (phospho-substrate readouts), FOXO1/p53 western blot, immunofluorescence (p53 localization), co-immunoprecipitation (p53-AKT), apoptosis assay Cellular and molecular life sciences : CMLS Medium 39847113
2025 PARP12 ADP-ribosylates viral RNA of chikungunya virus (positive-strand RNA virus), which inhibits translation in cell-free systems and infected fibroblasts, promotes more rapid viral RNA decay, and induces antiviral host response gene expression (acting as a novel pathogen-associated molecular pattern, PAMP). The viral macrodomain counteracts this RNA ribosylation. RNA ribosylation assay (PARP12), cell-free translation system, infected fibroblast translation assay, viral RNA decay assay, antiviral gene expression (qRT-PCR/RNA-seq), chikungunya virus infection model bioRxivpreprint Medium bio_10.1101_2025.07.18.665567
2025 PARP12 ADP-ribosylates approximately 150 mRNAs, including insulin mRNA, in MIN6 insulin-producing cells during inflammation. This mRNA ADP-ribosylation modifies transcript localization and halts translation, suggesting a post-transcriptional regulatory role in insulin production during insulitis. Proteomics/mass spectrometry, RNA ADP-ribosylation mapping (proteomics of RNA machinery), mRNA localization assay, translation assay, PARP12 induction by cytokines Research square (preprint)preprint Low 40470236
2024 In RA fibroblast-like synoviocytes, elevated trans-Golgi NAD+ (resulting from QPRT deficiency) suppresses TGN-resident PARP12, leading to mTORC1-mediated protein translation and Golgi expansion. This places PARP12 downstream of TGN NAD+ availability as a regulator of protein secretion. QPRT knockdown, NAD+ compartment measurement, mTORC1 activity assay, Golgi morphology analysis, RA mouse model with QPRT gene therapy bioRxiv (preprint)preprint Low bio_10.1101_2024.10.27.24316032

Source papers

Stage 0 corpus · 40 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2013 BMN 673, a novel and highly potent PARP1/2 inhibitor for the treatment of human cancers with DNA repair deficiency. Clinical cancer research : an official journal of the American Association for Cancer Research 412 23881923
2013 Genome-wide profiling of genetic synthetic lethality identifies CDK12 as a novel determinant of PARP1/2 inhibitor sensitivity. Cancer research 305 24240700
2014 Combined inhibition of Wee1 and PARP1/2 for radiosensitization in pancreatic cancer. Clinical cancer research : an official journal of the American Association for Cancer Research 135 25117293
2014 PARP12, an interferon-stimulated gene involved in the control of protein translation and inflammation. The Journal of biological chemistry 104 25086041
2018 PARP12 suppresses Zika virus infection through PARP-dependent degradation of NS1 and NS3 viral proteins. Science signaling 103 29921658
2019 A phase 1 study of veliparib, a PARP-1/2 inhibitor, with gemcitabine and radiotherapy in locally advanced pancreatic cancer. EBioMedicine 102 30635165
2017 PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions. Scientific reports 93 29070863
2015 E7449: A dual inhibitor of PARP1/2 and tankyrase1/2 inhibits growth of DNA repair deficient tumors and antagonizes Wnt signaling. Oncotarget 75 26513298
2013 A high-throughput screen identifies PARP1/2 inhibitors as a potential therapy for ERCC1-deficient non-small cell lung cancer. Oncogene 71 23934192
2021 HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications. Nature communications 63 34795260
2018 PARP12 (ARTD12) suppresses hepatocellular carcinoma metastasis through interacting with FHL2 and regulating its stability. Cell death & disease 40 30154409
2019 PARP-1/2 Inhibitor Olaparib Prevents or Partially Reverts EMT Induced by TGF-β in NMuMG Cells. International journal of molecular sciences 33 30691122
2016 Iodinated benzimidazole PARP radiotracer for evaluating PARP1/2 expression in vitro and in vivo. Nuclear medicine and biology 33 27689533
2021 ADP-ribosyltransferase PARP11 suppresses Zika virus in synergy with PARP12. Cell & bioscience 30 34187568
2020 Proton and photon radiosensitization effects of niraparib, a PARP-1/-2 inhibitor, on human head and neck cancer cells. Head & neck 30 32323895
2022 PKD-dependent PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 is required for E-cadherin transport from Golgi to plasma membrane. Proceedings of the National Academy of Sciences of the United States of America 29 34969853
2024 IRF1-mediated upregulation of PARP12 promotes cartilage degradation by inhibiting PINK1/Parkin dependent mitophagy through ISG15 attenuating ubiquitylation and SUMOylation of MFN1/2. Bone research 21 39465252
2023 PARP12 is required to repress the replication of a Mac1 mutant coronavirus in a cell- and tissue-specific manner. Journal of virology 21 37695054
2020 AMXI-5001, a novel dual parp1/2 and microtubule polymerization inhibitor for the treatment of human cancers. American journal of cancer research 18 32905466
2021 P-Glycoprotein (ABCB1/MDR1) Controls Brain Penetration and Intestinal Disposition of the PARP1/2 Inhibitor Niraparib. Molecular pharmaceutics 16 34730366
2021 Discovery of Quinazoline-2,4(1H,3H)-dione Derivatives Containing 3-Substituted Piperizines as Potent PARP-1/2 Inhibitors─Design, Synthesis, In Vivo Antitumor Activity, and X-ray Crystal Structure Analysis. Journal of medicinal chemistry 16 34748333
2022 Rational design, synthesis and biological evaluation of dual PARP-1/2 and TNKS1/2 inhibitors for cancer therapy. European journal of medicinal chemistry 15 35504210
2022 Identification of PARP12 Inhibitors By Virtual Screening and Molecular Dynamics Simulations. Frontiers in pharmacology 15 36016564
2024 Regulation of PARP1/2 and the tankyrases: emerging parallels. The Biochemical journal 9 39178157
2025 PARP12-mediated mono-ADP-ribosylation as a checkpoint for necroptosis and apoptosis. Proceedings of the National Academy of Sciences of the United States of America 8 40489618
2019 The oncoprotein DEK affects the outcome of PARP1/2 inhibition during mild replication stress. PloS one 7 31408463
2023 PARP12 regulates mouse oocyte meiotic maturation. Journal of cellular physiology 6 37305966
2023 Safety, Tolerability, and Pharmacokinetics of Senaparib, a Novel PARP1/2 Inhibitor, in Chinese Patients With Advanced Solid Tumors: A Phase I Trial. The oncologist 6 37338150
2022 PARP12 is required for mitochondrial function maintenance in thermogenic adipocytes. Adipocyte 5 35916471
2025 PARP12-mediated ADP-ribosylation contributes to breast cancer cell fate by regulating AKT activation and DNA-damage response. Cellular and molecular life sciences : CMLS 3 39847113
2024 Leveraging PARP-1/2 to Target Distant Metastasis. International journal of molecular sciences 3 39201718
2022 Absorption, distribution, metabolism, and excretion of [14C]Mefuparib (CVL218), a novel PARP1/2 inhibitor, in rats. Cancer chemotherapy and pharmacology 3 36283983
2021 Identification of poly(ADP-ribose)polymerase 1 and 2 (PARP1/2) as targets of andrographolide using an integrated chemical biology approach. Chemical communications (Cambridge, England) 2 34075974
2023 PARP12 is required to repress the replication of a Mac1 mutant coronavirus in a cell and tissue specific manner. bioRxiv : the preprint server for biology 1 37398292
2026 Functional characterization of short-isoform of PARP12 in the immune response to SVCV infection in common carp (Cyprinus carpio). Developmental and comparative immunology 0 41539453
2026 Tumor metabolic adaptation induced by L-asparaginase reveals a vulnerability to PARP1/2 inhibitor in B-cell lymphomas. Nature communications 0 41760625
2026 JPI-547, a novel dual inhibitor of PARP1/2 and tankyrase is more effective than first-generation PARP inhibitors in preclinical BRCA1/2-mutated cancer models. British journal of cancer 0 42092176
2025 Unveiling Promising PARP12 Inhibitors through Virtual Screening for Cancer Therapy. Current pharmaceutical design 0 40265429
2025 Insulin post-transcriptional regulation via PARP12-mediated ADP- ribosylation. Research square 0 40470236
2024 Screening and design of PARP12 inhibitors from traditional Chinese medicine small molecules using computational modeling and simulation. Journal of biomolecular structure & dynamics 0 39527026

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