Ask about this productRelated genes to: PARP9 Blocking Peptide
- Gene:
- PARP9 NIH gene
- Name:
- poly(ADP-ribose) polymerase family member 9
- Previous symbol:
- -
- Synonyms:
- BAL, BAL1
- Chromosome:
- 3q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-09-30
- Date modifiied:
- 2015-11-06
Related products to: PARP9 Blocking Peptide
Related articles to: PARP9 Blocking Peptide
- Evidence for persistent epigenetic changes in individuals who had a mild SARS-CoV-2 infection is limited, as most DNA methylation (DNAm) studies to date have focused on either the acute phase of infection or on the months following infection in severe cases requiring hospitalization. - Source: PubMed
Publication date: 2026/06/13
Matías-García Pamela RLai LiyeDelerue ThomasOhnmacht JochenStark Klaus JWarmerdam RobertKolodkin AlexeySix-Merker JuliaMangold NinaGünther KathrinO'Sullivan Marc PRauschenberger ArminBohn BarbaraBerger KlausFricke JuliaAhnert PeterFranke LudeKrüger RejkoGefeller OlafÜberla KlausHeid Iris MWagner Ralf Waldenberger MelaniePeters Annette - ADP-ribosylation is a reversible post-translational modification that regulates diverse cellular processes, including DNA damage repair, transcription, cell proliferation and innate immune responses, and is primarily catalyzed by members of the PARP family. While all 17 human PARPs contain a conserved C-terminal ADP-ribosyltransferase (ART) domain, only catalytically active members transfer ADP-ribose (ADPr) from nicotinamide adenine dinucleotide (NAD⁺) onto proteins or nucleic acids, and their N-terminal accessory domains, such as macro domains (MDs), WWE domains or RNA-binding motifs, mediate interactions that diversify PARP functions. Human PARP9 (hPARP9), known also as BAL1, is catalytically inactive due to sequence variations in catalytically important residues in the ART domain, but plays crucial roles in antiviral and antibacterial defense, stress responses and tumor progression through its heterodimeric interaction with the E3 ubiquitin ligase DTX3L. hPARP9 contains two tandem MDs (MD1 and MD2), with MD1 acting as a MacroD-type hydrolase "eraser" of mono-ADP-ribosylation (MARylation), while MD2 functions as an ADPr "reader". Their different role in the ADP-ribosylation pathway highlights the importance of structural and functional characterization for understanding ADPr-mediated cellular signaling. In this study, we report the NMR backbone and side-chain resonance assignments of hPARP9 MD1 in both apo and ADPr bound states. In addition, the secondary structure predictions using TALOS+ server and the Chemical Shift Perturbation (CSP) analysis upon ADPr binding are presented. The latter illustrates the MD substrate's accommodation mode and identifies the residues involved in ADPr binding, thus related to MDs' hydrolytic activity. - Source: PubMed
Publication date: 2026/06/12
Moschidi DanaiFourkiotis Nikolaos KTsatsouli Sofia-AntigoniTsika Aikaterini CSpyroulias Georgios A - Targeted radionuclide therapy with Lu-PSMA-617 prolongs radiographical progression-free survival in prostate-specific membrane antigen (PSMA)-positive metastatic castration-resistant prostate cancer (mCRPC), yet 13% of patients develop symptomatic skeletal events. The authors hypothesized that hemoglobin-based oxygen carriers (HBOCs) could potentiate Lu-PSMA-617 by reprogramming bone marrow (BM) immunity.Using PSMA-expressing xenografts, they demonstrated that concomitant HBOC administration significantly reduced tumor volume without increasing systemic toxicity. To dissect the underlying mechanism, the authors performed high-resolution single-cell RNA sequencing of murine BM.HBOC treatment markedly expanded mature neutrophils, plasmacytoid dendritic cells, classical monocytes, natural killer T cells, and mature B cells, while concomitantly upregulating DNA damage repair genes such as , , and within these subsets. Gene set enrichment analysis confirmed significant activation of DNA damage response pathways, implying enhanced cellular radioresistance and improved tolerance to β-particle irradiation. Thus, HBOCs improve Lu-PSMA-617 antitumor efficacy indirectly via immune-subset expansion and DNA-repair reinforcement, offering a clinically feasible and safe strategy to optimize combination protocols for patients with mCRPC. - Source: PubMed
Publication date: 2026/05/22
Qu DanyueShao ChenyiJi XinyuanHuang YichiTian ChenLi JiazeZhou HuShi YileiWang HongLiu JiaxinZhao Yu - Ageing is accompanied by progressive microvascular dysfunction, a key determinant of organ performance and longevity. The molecular drivers of this process remain incompletely defined, and the mechanisms by which exercise counters vascular ageing are unclear. This study investigated whether exercise-regulated long noncoding RNAs (lncRNAs) contribute to microvascular ageing and age-related cardiac dysfunction. - Source: PubMed
Publication date: 2026/05/19
Li HaoboXiao XiaoZhou YirongZhang YajingKang JiayiYuan ZixunHe JiaqiGuerra JustinLerchenmüller CarolinMargulies Kenneth BAguirre Aaron DRoh Jason DRosenzweig Anthony - Androgen receptor (AR) signalling is central to both normal prostate physiology and prostate cancer (PCa) progression. Its activity is tightly regulated by localization, transcriptional control, and post-translational modifications. Among these, poly (ADP-ribose) polymerase (PARP) mediated ADP-ribosylation has emerged as a key regulator. Multisite cysteine mono-ADP-ribosylation of AR by PARP7 modulates its function. Molecular recognition of ADP-ribosyl-cysteine by PARP9/DTX3L influences AR-driven gene expression. Importantly, defects in homologous recombination repair (HRR) genes have made PARP inhibitors (PARPi) an effective treatment for BRCA (Breast cancer susceptibility genes 1 and 2)-mutated metastatic castration-resistant prostate cancer (mCRPC). Clinical trials such as TALAPRO-2 show that combining PARPi with AR signalling inhibitors can be effective; however, their benefit in tumours without HRR mutations remains unclear. PARP enzymes regulate AR via MARylation and PARylation, with inhibitors such as Olaparib, which disrupts AR-PARP crosstalk. In this review, we present current knowledge on the interplay between ADP-ribosylation and AR signalling in prostate cancer, emphasizing the roles of distinct PARP enzymes in shaping AR activity and therapeutic response. Herein, we focus on the combined contributions of MARylation and PARylation to prostate tumorigenesis. We also discuss how this complex regulatory network may contribute to the development of advanced prostate cancer therapies in the future. This could improve PARP inhibitor and AR signalling inhibitor combinations and allow more patients to benefit from them. - Source: PubMed
Publication date: 2026/04/14
Reddy Gali Sri Venkata Sai RishmaSamanta KrishnaKar Pulak