ArticleNucleic acids research2017
Structural basis for substrate binding and catalytic mechanism of a human RNA:m5C methyltransferase NSun6.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 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
80 citing papers in PubMed, 128 citations in OpenAlex.
- Emerging roles of RNA N5-methylcytosine modification in reproductive physiology and gynecological diseases.Epigenetics · 2026Review
- RNA-Binding Peptide Influences Epitranscriptomic Regulation by Preferentially Binding to Unmodified RNAs Targeted by NSUN2.Biomolecules · 2026Article
- AL398, A Novel NSUN6 Inhibitor, Attenuates Epithelial-Mesenchymal Transition and Metastasis in Endometrial Cancer by Abrogating m5C-Dependent Stabilization of Snail mRNA.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- TRDMT1 slows lung cancer growth by stabilizing TFRC mRNA and triggering ferroptosis cell death.The Journal of biological chemistry · 2026Article
- Review
- RModBlock antisense oligonucleotides as a universal tool for precise and efficient inhibition of RNA modifications.Nature biomedical engineering · 2026Article
- Substrate selectivity of the human RNA mNature · 2026Article
- Oxidative stress-driven mRedox biology · 2026Article
- tRNA methylation: functional insights and epitranscriptomic regulation.Cell communication and signaling : CCS · 2026Review
- Structure-driven RNA remodeling underlies broad substrate recognition by NSUN2.Science China. Life sciences · 2026Article
- mAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- RNA Methylation in Cancer Metabolism: from Mechanisms to Therapeutic Opportunities.International journal of biological sciences · 2026Review
- NSUN4-mediated m5C RNA methylation protects retinal cells against excitotoxic injury via the SHH signaling pathway.PloS one · 2026Article
- Transcription factor ATF3 positively regulates the transcription of NSUN6 gene.Molecular biology reports · 2025Article
- NSUN7 is a catalytically inactive RNA mNature communications · 2025Article
- Advances in RNA modification in myocardial fibrosis (Review).International journal of molecular medicine · 2025Review
- A comprehensive tRNA pseudouridine map uncovers targets dependent on human stand-alone pseudouridine synthases.Nature cell biology · 2025Article
- Targeting tRNA methyltransferases: from molecular mechanisms to drug discovery.Science China. Life sciences · 2025Review
- A cohort of mRNAs undergo high-stoichiometry NSUN6-mediated site-specific mNature communications · 2025Article
- The diverse landscape of RNA modifications in cancer development and progression.Genes & genomics · 2025Review
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
5-methylcytosine (m5C) modifications of RNA are ubiquitous in nature and play important roles in many biological processes such as protein translational regulation, RNA processing and stress response. Aberrant expressions of RNA:m5C methyltransferases are closely associated with various human diseases including cancers. However, no structural information for RNA-bound RNA:m5C methyltransferase was available until now, hindering elucidation of the catalytic mechanism behind RNA:m5C methylation. Here, we have solved the structures of NSun6, a human tRNA:m5C methyltransferase, in the apo form and in complex with a full-length tRNA substrate. These structures show a non-canonical conformation of the bound tRNA, rendering the base moiety of the target cytosine accessible to the enzyme for methylation. Further biochemical assays reveal the critical, but distinct, roles of two conserved cysteine residues for the RNA:m5C methylation. Collectively, for the first time, we have solved the complex structure of a RNA:m5C methyltransferase and addressed the catalytic mechanism of the RNA:m5C methyltransferase family, which may allow for structure-based drug design toward RNA:m5C methyltransferase-related diseases.
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.