PARP3, Human Recombinant Protein
- Known as:
- PARP3, Human Recombinant Protein
- Catalog number:
- 80503
- Product Quantity:
- 10 µg
- Category:
- -
- Supplier:
- BPS Bioscience
- Gene target:
- PARP3 Human Recombinant Protein
Related genes to: PARP3, Human Recombinant Protein
- Gene:
- PARP3 NIH gene
- Name:
- poly(ADP-ribose) polymerase family member 3
- Previous symbol:
- ADPRTL3
- Synonyms:
- ADPRT3, IRT1, hPARP-3, pADPRT-3
- Chromosome:
- 3p21.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-24
- Date modifiied:
- 2015-11-06
Related products to: PARP3, Human Recombinant Protein
Related articles to: PARP3, Human Recombinant Protein
- Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) exploits host cellular machinery to support its replication. Members of the host poly(ADP-ribose) polymerase (PARP) family regulate the DNA damage response and have been implicated in both antiviral and proviral processes. In this study, we investigated the potential role of PARP3 in SARS-CoV-2 replication in VeroE6/Rep3 cells. siRNA-mediated knockdown of PARP3 reduced viral subgenomic RNA (sgRNA) levels and reporter activity, whereas PARP3 overexpression enhanced these processes, suggesting that PARP3 promotes SARS-CoV-2 replication. In addition, PARP3 expression was increased in SARS-CoV-2-infected Calu-3 cells and in cells expressing SARS-CoV-2 nucleocapsid protein, suggesting that the nucleocapsid protein contributes to PARP3 upregulation during infection. Co-immunoprecipitation and immunofluorescence analyses revealed that PARP3 associates with the nucleocapsid protein and redistributes to the cytoplasm in nucleocapsid-expressing cells. Screening of a PARP inhibitor library identified venadaparib as a compound that reduced SARS-CoV-2 sgRNA levels and reporter activity in VeroE6/Rep3 cells with limited cytotoxicity under the condition tested. We further found that venadaparib reduced the interaction between PARP3 and the nucleocapsid protein. Molecular docking analysis further suggested that venadaparib can bind to the PARP3 catalytic domain. Collectively, these findings support a model in which PARP3 facilitates SARS-CoV-2 replication through its interaction with the viral nucleocapsid protein and suggest that venadaparib warrants further evaluation as a host-directed antiviral candidate. - Source: PubMed
Publication date: 2026/08/31
Adyaksa Dewa Nyoman MurtiRhamadianti Aulia FitriDeng LinAbe TakayukiMatsui ChiekoShoji Ikuo - Dual inhibition of Polθ and PARP1 represents a promising precision therapy strategy for HR-deficient tumors. While our first-generation Polθ/PARP1 dual inhibitor 4 provided proof-of-concept, its further development was hampered by poor selectivity over PARP2 and metabolic instability. Herein, we describe a structure-guided optimization that pioneers the integration of PARP1-selective pharmacophores. This effort culminated in the discovery of compound PP-048 (23), a second-generation dual inhibitor with single-digit nanomolar potency against Polθ and PARP1 (IC50 = 4.9 nM and 6.8 nM, respectively) and >226-fold selectivity over PARP2, PARP3, PARP5a/b, and PARP7. Notably, PP-048 displayed markedly improved hepatic stability and favorable oral systemic exposure. In an MDA-MB-436 xenograft model, PP-048 (10 mg/kg) achieved marked tumor growth inhibition (TGI = 91%) without eliciting the hematologic toxicity associated with PARP2 inhibition. To our knowledge, PP-048 represents the first reported PARP1-isoform-selective dual inhibitor, establishing a strategic foundation for development of this emerging class of inhibitors. - Source: PubMed
Ma LuyuZhong MingzheChang YingxuanLuo MingjinLiu XinyanGe XiaofanXu SitianZhang YunLiu ZiyeXiang HuaLuo Guoshun - Cancer cells exploit DNA repair to overcome damage and errors induced by rapid proliferation and repressed checkpoints. Thus, the loss of one DNA repair protein can make tumors more susceptible to inhibition of other repair pathways. Here, using in silico methodologies and high-content genetic and cell survival screens, we found that the antimalarial drug quinacrine impaired the DNA damage response (DDR) in multiple cancer cell lines. Quinacrine disrupted the interaction of the stress-response protein NDRG1 with the major segregase VCP, which in turn promoted the degradation of the E3 ubiquitin ligase RNF8 and other proteins that mediate the recruitment of the critical DDR protein 53BP1 to sites of DNA damage. This impaired recruitment of 53BP1 caused increases in the DNA damage marker γH2AX. High expression in tumors correlated with poor survival in patients, and high expression in various cancer cell lines correlated with quinacrine sensitivity. Colorectal carcinoma cells were particularly vulnerable to pharmacological or genetic inhibition of NDRG1, and high expression and mutations in and resulted in synthetic lethality. Our findings identify combination genetic markers that might be therapeutically exploited in colon cancer, as well as provide a platform for such discovery in distinct cancer types. - Source: PubMed
Publication date: 2026/07/21
Mkrtchyan Garik VVeviorskiy AlexanderMeisen Zarah GPetr Michael AMercurio Tobias ClausenBakula DanielaSykora PeterKuo Li-WeiRosenthal Dean SSimbulan-Rosenthal Cynthia MZhang PeiranTang QiuqiongOsipov Andreyan NOzerov Ivan VAliper AlexZhavoronkov AlexScheibye-Knudsen Morten - Epileptogenesis transforms a healthy brain into an epileptic network, yet the temporal and cell-type-specific molecular events driving this transition remain poorly defined. Neuron-glia interactions are essential in this process, but no study has systematically charted their transcriptional dynamics from the acute insult to chronic epilepsy. - Source: PubMed
Publication date: 2026/06/21
Berger Toni ChristophVigeland Magnus DehliHjorthaug Hanne SagsveenNome Cecilie GjessingBeier Christoph PatrickTaubøll ErikSelmer Kaja KristineHeuser Kjell - - Source: PubMed
Publication date: 2026/05/29
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