ReviewRNA biology
Taming free energy landscapes with RNA chaperones.
Review in RNA biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 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.
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
72 citing papers in PubMed.
- Identification of proteins exhibitingRNA biology · 2026Article
- RNA and proteins joined up at the Origins of Life: Persistence is the point.bioRxiv : the preprint server for biology · 2026Article
- FRET-guided selection of RNA 3D structures.Nucleic acids research · 2026Article
- Ubiquitous low-energy RNA fluctuations and energetic coupling measured by chemical probing.bioRxiv : the preprint server for biology · 2026Article
- tRNA-modifying enzymes in bacterial stress adaptation.Open biology · 2025Review
- Structural flexibility in the ordered domain of the dengue virus strain 2 capsid protein is critical for chaperoning viral RNA replication.Cellular and molecular life sciences : CMLS · 2025Article
- Consistent features observed in structural probing data of eukaryotic RNAs.NAR genomics and bioinformatics · 2025Article
- Disassembly of unstable RNA structures by an E. coli DEAD-box chaperone accelerates ribosome assembly.Nucleic acids research · 2025Article
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.Nature communications · 2025Article
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.bioRxiv : the preprint server for biology · 2024Article
- Putting It All Together: The Roles of Ribosomal Proteins in Nucleolar Stages of 60S Ribosomal Assembly in the YeastBiomolecules · 2024Review
- NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity.Nature communications · 2024Article
- Moderate activity of RNA chaperone maximizes the yield of self-spliced pre-RNA in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- How does RNA fold dynamically?Journal of molecular biology · 2022Review
- Rotavirus RNA chaperone mediates global transcriptome-wide increase in RNA backbone flexibility.Nucleic acids research · 2022Article
- Action and function of helicases on RNA G-quadruplexes.Methods (San Diego, Calif.) · 2022Review
- Peptides before and during the nucleotide world: an origins story emphasizing cooperation between proteins and nucleic acids.Journal of the Royal Society, Interface · 2022Review
- Detection ofLife (Basel, Switzerland) · 2021Article
- The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements.Nucleic acids research · 2021Article
- Transcription complexes as RNA chaperones.Transcription · 2021Article
12 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
1 author.
Funding
Abstract
Many non-coding RNAs fold into complex three-dimensional structures, yet the self-assembly of RNA structure is hampered by mispairing, weak tertiary interactions, electrostatic barriers, and the frequent requirement that the 5' and 3' ends of the transcript interact. This rugged free energy landscape for RNA folding means that some RNA molecules in a population rapidly form their native structure, while many others become kinetically trapped in misfolded conformations. Transient binding of RNA chaperone proteins destabilize misfolded intermediates and lower the transition states between conformations, producing a smoother landscape that increases the rate of folding and the probability that a molecule will find the native structure. DEAD-box proteins couple the chemical potential of ATP hydrolysis with repetitive cycles of RNA binding and release, expanding the range of conditions under which they can refold RNA structures.
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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.