ArticleScientific reports2016
Characterization of the DNA dependent activation of human ARTD2/PARP2.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 47 citations in OpenAlex.
- Structural basis of PARP2 recognition of nucleosomal DNA breaks and inhibitor trapping.Nucleic acids research · 2026Article
- The BRCT domain enhances DNA binding and catalytic efficiency of fungal PARPs.Nature communications · 2026Article
- PARP-2 catalytic activity drives replication-ICL repair in an allele-specific manner during germline development.PLoS genetics · 2026Article
- Yeast as a Platform to Dissect Poly(ADP-Ribose) Polymerase Function fromInternational journal of molecular sciences · 2026Article
- Discovery of Fused Isoquinolinone/Triazole as a Scaffold for Tankyrase and PARP Inhibition.Journal of medicinal chemistry · 2026Article
- Poly(ADP-ribose)polymerase 2 is zinc-dependent enzyme and nucleosome reorganizer.Cellular and molecular life sciences : CMLS · 2025Article
- PARP2 Catalytic Activity Is Allosterically Stimulated by Binding to the c-KIT1 G-Quadruplex.ACS omega · 2025Article
- Specific and shared biological functions of PARP2 - is PARP2 really a lil' brother of PARP1?Expert reviews in molecular medicine · 2024Review
- PARP2 promotes Break Induced Replication-mediated telomere fragility in response to replication stress.Nature communications · 2024Article
- High-throughput screening assay for PARP-HPF1 interaction inhibitors to affect DNA damage repair.Scientific reports · 2024Article
- Single-molecule force spectroscopy reveals binding and bridging dynamics of PARP1 and PARP2 at DNA double-strand breaks.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- PARP2 poly(ADP-ribosyl)ates nuclear factor erythroid 2-related factor 2 (NRF2) affecting NRF2 subcellular localization.Scientific reports · 2023Article
- Predicted coronavirus Nsp5 protease cleavage sites in the human proteome.BMC genomic data · 2022Article
- Inhibitors of PARP: Number crunching and structure gazing.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- ADP-ribosylation of DNA and RNA.DNA repair · 2021Review
- Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition.Nature communications · 2021Article
- ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function.Nucleic acids research · 2021Review
- The contribution of PARP1, PARP2 and poly(ADP-ribosyl)ation to base excision repair in the nucleosomal context.Scientific reports · 2021Article
- Nuclear PARPs and genome integrity.Genes & development · 2020Review
- Nonspecific Binding of RNA to PARP1 and PARP2 Does Not Lead to Catalytic Activation.Biochemistry · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human ADP-ribosyltransferase 2 (ARTD2/PARP2) is an enzyme catalyzing a post-translational modification, ADP-ribosylation. It is one of the three DNA dependent ARTDs in the 17 member enzyme family. ADP-ribosylation catalyzed by ARTD2 is involved in the regulation of multiple cellular processes such as control of chromatin remodeling, transcription and DNA repair. Here we used a combination of biochemical and biophysical methods to elucidate the structure and function of ARTD2. The solution structures revealed the binding mode of the ARTD2 monomer and dimer to oligonucleotides that mimic damaged DNA. In the complex, DNA binds between the WGR domain and the catalytic fragment. The binding mode is supported by biophysical data that indicate all domains contribute to DNA binding. Also, our study showed that ARTD2 is preferentially activated by short 5'-phosphorylated DNA oligonucleotides. We demonstrate that the N-terminus functions as a high-affinity DNA-binding module, while the WGR domain contributes to DNA binding specificity and subsequent catalytic activation. Our data further suggest that ARTD2 would function in double strand break repair as a dimeric module, while in single strand break repair it would function as a monomer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.