ArticleNature communications2019
Cryo-EM structure of a 40 kDa SAM-IV riboswitch RNA at 3.7 Å resolution.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 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
86 citing papers in PubMed, 140 citations in OpenAlex.
- EXPECTATION-MAXIMIZATION FOR STRUCTURE DETERMINATION DIRECTLY FROM CRYO-EM MICROGRAPHS.Inverse problems and imaging (Springfield, Mo.) · 2027Article
- Self-splicing and cyclization mechanisms of the full-length Anabaena pre-tRNA.Nature chemical biology · 2026Article
- Biomolecular Corona Remodelling ofJournal of extracellular biology · 2026Article
- High-resolution cryo-EM structures of small protein-ligand complexes near the theoretical size limit.Nature communications · 2026Article
- Scaffolds with optimized quaternary symmetry for de novo cryoEM structure determination of small RNAs.Nature methods · 2026Article
- Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA.Nucleic acids research · 2026Article
- Article
- DNP-Enhanced Magic Angle Spinning Solid-State NMR Spectroscopy to Determine RNA-Ligand Interactions.Journal of the American Chemical Society · 2026Article
- Solid-state nanopore sensing reveals conformational changes induced by a mutation in a neuron-specific tRNAArg.Nucleic acids research · 2026Article
- Structural determination of small proteins by cryo-EM using a coiled coil module strategy.Scientific reports · 2025Article
- An Empirical Biasing Force Constant to Minimize Overfitting in Cryo-EM Flexible Fitting Refinement.Journal of chemical information and modeling · 2025Article
- Analysis of natural structures and chemical mapping data reveals local stability compensation in RNA.Nucleic acids research · 2025Article
- Molecular insights into de novo small-molecule recognition by an intron RNA structure.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- RNA sample optimization for cryo-EM analysis.Nature protocols · 2025Review
- DeepRNA-Twist: language-model-guided RNA torsion angle prediction with attention-inception network.Briefings in bioinformatics · 2025Article
- Ligand-binding pockets in RNA and where to find them.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Analysis of natural structures and chemical mapping data reveals local stability compensation in RNA.bioRxiv : the preprint server for biology · 2025Article
- Investigating the interplay between RNA structural dynamics and RNA chemical probing experiments.Nucleic acids research · 2025Article
- Complex Water Networks Visualized through 2.2-2.3 Å Cryogenic Electron Microscopy of RNA.bioRxiv : the preprint server for biology · 2025Article
- RNA folding kinetics control riboswitch sensitivity in vivo.Nature communications · 2025Article
26 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
9 authors at 4 institutions in 1 country.
Funding
Abstract
Specimens below 50 kDa have generally been considered too small to be analyzed by single-particle cryo-electron microscopy (cryo-EM). The high flexibility of pure RNAs makes it difficult to obtain high-resolution structures by cryo-EM. In bacteria, riboswitches regulate sulfur metabolism through binding to the S-adenosylmethionine (SAM) ligand and offer compelling targets for new antibiotics. SAM-I, SAM-I/IV, and SAM-IV are the three most commonly found SAM riboswitches, but the structure of SAM-IV is still unknown. Here, we report the structures of apo and SAM-bound SAM-IV riboswitches (119-nt, ~40 kDa) to 3.7 Å and 4.1 Å resolution, respectively, using cryo-EM. The structures illustrate homologies in the ligand-binding core but distinct peripheral tertiary contacts in SAM-IV compared to SAM-I and SAM-I/IV. Our results demonstrate the feasibility of resolving small RNAs with enough detail to enable detection of their ligand-binding pockets and suggest that cryo-EM could play a role in structure-assisted drug design for RNA.
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.