ArticleBiochemistry2011
Biochemical characterization of metnase's endonuclease activity and its role in NHEJ repair.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 55 citations in OpenAlex.
- Somatic mutations and genome mosaicism in aging and disease.Experimental & molecular medicine · 2026Review
- Epistasis between mutator alleles contributes to germline mutation spectrum variability in laboratory mice.eLife · 2024Article
- Epistasis between mutator alleles contributes to germline mutation spectra variability in laboratory mice.bioRxiv : the preprint server for biology · 2023Article
- Assessing the Effect of Histone Deacetylase Inhibitors on DNA Double-Strand Break Repair by Nonhomologous End Joining.Methods in molecular biology (Clifton, N.J.) · 2023Article
- SETMAR, a case of primate co-opted genes: towards new perspectives.Mobile DNA · 2022Review
- Metnase and EEPD1: DNA Repair Functions and Potential Targets in Cancer Therapy.Frontiers in oncology · 2022Review
- Structure, Activity, and Function of SETMAR Protein Lysine Methyltransferase.Life (Basel, Switzerland) · 2021Review
- Repair of DNA Double-Strand Breaks by the Nonhomologous End Joining Pathway.Annual review of biochemistry · 2021Review
- SETMAR Shorter Isoform: A New Prognostic Factor in Glioblastoma.Frontiers in oncology · 2021Article
- New Faces of old Friends: Emerging new Roles of RNA-Binding Proteins in the DNA Double-Strand Break Response.Frontiers in molecular biosciences · 2021Review
- Distinct roles of structure-specific endonucleases EEPD1 and Metnase in replication stress responses.NAR cancer · 2020Article
- The roles of the human SETMAR (Metnase) protein in illegitimate DNA recombination and non-homologous end joining repair.DNA repair · 2019Article
- Endonuclease EEPD1 Is a Gatekeeper for Repair of Stressed Replication Forks.The Journal of biological chemistry · 2017Article
- SETMAR isoforms in glioblastoma: A matter of protein stability.Oncotarget · 2017Article
- Metnase Mediates Loading of Exonuclease 1 onto Single Strand Overhang DNA for End Resection at Stalled Replication Forks.The Journal of biological chemistry · 2017Article
- Crystallization of and selenomethionine phasing strategy for a SETMAR-DNA complex.Acta crystallographica. Section F, Structural biology communications · 2016Article
- hPso4/hPrp19: a critical component of DNA repair and DNA damage checkpoint complexes.Oncogene · 2016Review
- PREVENTING THE CHROMOSOMAL TRANSLOCATIONS THAT CAUSE CANCER.Transactions of the American Clinical and Climatological Association · 2016Article
- A Proteomic Strategy Identifies Lysine Methylation of Splicing Factor snRNP70 by the SETMAR Enzyme.The Journal of biological chemistry · 2015Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Metnase (SETMAR) is a SET-transposase fusion protein that promotes nonhomologous end joining (NHEJ) repair in humans. Although both SET and the transposase domains were necessary for its function in DSB repair, it is not clear what specific role Metnase plays in the NHEJ. In this study, we show that Metnase possesses a unique endonuclease activity that preferentially acts on ssDNA and ssDNA-overhang of a partial duplex DNA. Cell extracts lacking Metnase poorly supported DNA end joining, and addition of wt-Metnase to cell extracts lacking Metnase markedly stimulated DNA end joining, while a mutant (D483A) lacking endonuclease activity did not. Given that Metnase overexpression enhanced DNA end processing in vitro, our finding suggests a role for Metnase's endonuclease activity in promoting the joining of noncompatible ends.
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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.