ArticleThe Journal of biological chemistry2015
Human DNA Exonuclease TREX1 Is Also an Exoribonuclease That Acts on Single-stranded RNA.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Single-dose radiotherapy is more effective than fractionation when combined with anti-PD-1 immunotherapy in glioblastoma.Scientific reports · 2025Article
- Prevalence and impact of molecular variation in the three-prime repair exonuclease 1 TREX1 and its implications for oncology.Human genomics · 2025Article
- Effect of methyl DNA adducts on 3'-5' exonuclease activity of human TREX1.The Biochemical journal · 2025Article
- DNA-sensing pathways in health, autoinflammatory and autoimmune diseases.Nature immunology · 2024Review
- Structure-specific nucleases in genome dynamics and strategies for targeting cancers.Journal of molecular cell biology · 2024Review
- The multiple faces of cGAS-STING in antitumor immunity: prospects and challenges.Medical review (2021) · 2024Review
- Replicative senescence and high glucose induce the accrual of self-derived cytosolic nucleic acids in human endothelial cells.Cell death discovery · 2024Article
- Three Prime Repair Exonuclease 1 preferentially degrades the integration-incompetent HIV-1 DNA through favorable kinetics, thermodynamic, structural and conformational properties.bioRxiv : the preprint server for biology · 2024Article
- Association of TREX1 polymorphism with disease progression in human immunodeficiency virus type-1 (HIV-1) infected patients.Virus genes · 2023Article
- Molecular insight into the specific enzymatic properties of TREX1 revealing the diverse functions in processing RNA and DNA/RNA hybrids.Nucleic acids research · 2023Article
- TREX1 cytosolic DNA degradation correlates with autoimmune disease and cancer immunity.Clinical and experimental immunology · 2023Article
- Nucleic Acid Sensing in the Tumor Vasculature.Cancers · 2021Review
- TREX1 as a Novel Immunotherapeutic Target.Frontiers in immunology · 2021Article
- The Role of Cutaneous Type I IFNs in Autoimmune and Autoinflammatory Diseases.Journal of immunology (Baltimore, Md. : 1950) · 2020Review
- Tackling Resistance to Cancer Immunotherapy: What Do We Know?Molecules (Basel, Switzerland) · 2020Review
- Review
- Biology of RNA Surveillance in Development and Disease.Trends in cell biology · 2019Review
- Article
- Astrocytes, an active player in Aicardi-Goutières syndrome.Brain pathology (Zurich, Switzerland) · 2018Review
- Structural basis for overhang excision and terminal unwinding of DNA duplexes by TREX1.PLoS biology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
3' repair exonuclease 1 (TREX1) is a known DNA exonuclease involved in autoimmune disorders and the antiviral response. In this work, we show that TREX1 is also a RNA exonuclease. Purified TREX1 displays robust exoribonuclease activity that degrades single-stranded, but not double-stranded, RNA. TREX1-D200N, an Aicardi-Goutieres syndrome disease-causing mutant, is defective in degrading RNA. TREX1 activity is strongly inhibited by a stretch of pyrimidine residues as is a bacterial homolog, RNase T. Kinetic measurements indicate that the apparent Km of TREX1 for RNA is higher than that for DNA. Like RNase T, human TREX1 is active in degrading native tRNA substrates. Previously reported TREX1 crystal structures have revealed that the substrate binding sites are open enough to accommodate the extra hydroxyl group in RNA, further supporting our conclusion that TREX1 acts on RNA. These findings indicate that its RNase activity needs to be taken into account when evaluating the physiological role of TREX1.
Indexed as
Identifiers
What OpenQuestion holds
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.