ArticleNucleic acids research2012
Structure and activity of the only human RNase T2.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Inhibition of a magnesium-sensitive double-stranded RNA clearance machinery boosts cancer immunotherapy.Cell research · 2026Article
- RNASET2 degrades mRNAs that protect against lipotoxicity.Molecular metabolism · 2026Article
- Mechanical Wounding Induces Rapid RNA-Degrading Activity Mediated by the S-like Ribonuclease PvRNS2 in Common Bean.Plants (Basel, Switzerland) · 2026Article
- tRNA-derived RNA processing in sperm transmits non-genetically inherited phenotypes to offspring in C. elegans.Nature communications · 2026Article
- Laccaria bicolor adapts to phosphate deficiency at the developmental, transcriptional and metabolic levels.Mycorrhiza · 2025Article
- The lysosomal catabolism of nucleic acids-critical regulators of the innate immune system.Nucleic acids research · 2025Review
- Small RNA and Toll-like receptor interactions: origins and disease mechanisms.Trends in biochemical sciences · 2025Review
- Article
- Structural analysis of PLD3 reveals insights into the mechanism of lysosomal 5' exonuclease-mediated nucleic acid degradation.Nucleic acids research · 2024Article
- Epididymal RNase T2 contributes to astheno-teratozoospermia and intergenerational metabolic disorder through epididymosome-sperm interaction.BMC medicine · 2023Article
- The Potential Role of the T2 Ribonucleases in TME-Based Cancer Therapy.Biomedicines · 2023Review
- Ribonuclease T2 represents a distinct circularly permutated version of the BECR RNases.Protein science : a publication of the Protein Society · 2023Article
- Human RNASET2: A Highly Pleiotropic and Evolutionary Conserved Tumor Suppressor Gene Involved in the Control of Ovarian Cancer Pathogenesis.International journal of molecular sciences · 2022Review
- From Intestinal Epithelial Homeostasis to Colorectal Cancer: Autophagy Regulation in Cellular Stress.Antioxidants (Basel, Switzerland) · 2022Review
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- A 5' tRNA-Ala-derived small RNA regulates anti-fungal defense in plants.Science China. Life sciences · 2022Article
- Host Defence RNases as Antiviral Agents against Enveloped Single Stranded RNA Viruses.Virulence · 2021Review
- Increased S1P induces S1PR2 internalization to blunt the sensitivity of colorectal cancer to 5-fluorouracil via promoting intracellular uracil generation.Acta pharmacologica Sinica · 2021Article
- 3D Reconstruction ofInternational journal of molecular sciences · 2020Article
- Purification and Use of tRNA for Enzymatic Post-translational Addition of Amino Acids to Proteins.STAR protocols · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in the gene of human RNase T2 are associated with white matter disease of the human brain. Although brain abnormalities (bilateral temporal lobe cysts and multifocal white matter lesions) and clinical symptoms (psychomotor impairments, spasticity and epilepsy) are well characterized, the pathomechanism of RNase T2 deficiency remains unclear. RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans. In recent years, new functions such as tumor suppressing properties of RNase T2 have been reported that are independent of its catalytic activity. We determined the X-ray structure of human RNase T2 at 1.6 Å resolution. The α+β core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences. The catalytic features of RNase T2 in presence of bivalent cations were analyzed and the structural consequences of known clinical mutations were investigated. Our data provide further insight into the function of human RNase T2 and may prove useful in understanding its mode of action independent of its enzymatic activity.
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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.