ArticleScience (New York, N.Y.)2013
A guanosine-centric mechanism for RNA chaperone function.
Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 49 citations in OpenAlex.
- Effect of TAR hairpin stabilization on HIV-1 reverse transcription.Journal of virology · 2026Article
- SARS-CoV-2 nucleocapsid protein variants have differential RNA chaperone activity.The FEBS journal · 2026Article
- Inosine misincorporation into mRNA triggers the integrated stress response and activates an innate immune gene expression signature.bioRxiv : the preprint server for biology · 2026Article
- Picornavirus 2C proteins: structure-function relationships and interactions with host factors.Frontiers in cellular and infection microbiology · 2024Review
- Structural maturation of the HIV-1 RNA 5' untranslated region by Pr55RNA biology · 2022Article
- SHAPE Directed Discovery of New Functions in Large RNAs.Accounts of chemical research · 2021Review
- Predictions and analyses of RNA nearest neighbor parameters for modified nucleotides.Nucleic acids research · 2020Article
- Significant Differences in RNA Structure Destabilization by HIV-1 GagDp6 and NCp7 Proteins.Viruses · 2020Article
- Disordered RNA chaperones can enhance nucleic acid folding via local charge screening.Nature communications · 2019Article
- Stability of RNA duplexes containing inosine·cytosine pairs.Nucleic acids research · 2018Article
- Retroviral nucleocapsid proteins and DNA strand transfers.Biochimie open · 2018Review
- Stability of local secondary structure determines selectivity of viral RNA chaperones.Nucleic acids research · 2018Article
- Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018Review
- The Host Factor AUF1 p45 Supports Flavivirus Propagation by Triggering the RNA Switch Required for Viral Genome Cyclization.Journal of virology · 2018Article
- Human Norovirus NS3 Has RNA Helicase and Chaperoning Activities.Journal of virology · 2018Article
- The loss of a hydrogen bond: Thermodynamic contributions of a non-standard nucleotide.Nucleic acids research · 2017Article
- Mechanistic differences between HIV-1 and SIV nucleocapsid proteins and cross-species HIV-1 genomic RNA recognition.Retrovirology · 2016Article
- Arginine methylation enhances the RNA chaperone activity of the West Nile virus host factor AUF1 p45.RNA (New York, N.Y.) · 2016Article
- Characterizing RNA structures in vitro and in vivo with selective 2'-hydroxyl acylation analyzed by primer extension sequencing (SHAPE-Seq).Methods (San Diego, Calif.) · 2016Article
- The RNA chaperone activity of the Trypanosoma brucei editosome raises the dynamic of bound pre-mRNAs.Scientific reports · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
RNA chaperones are ubiquitous, heterogeneous proteins essential for RNA structural biogenesis and function. We investigated the mechanism of chaperone-mediated RNA folding by following the time-resolved dimerization of the packaging domain of a retroviral RNA at nucleotide resolution. In the absence of the nucleocapsid (NC) chaperone, dimerization proceeded through multiple, slow-folding intermediates. In the presence of NC, dimerization occurred rapidly through a single structural intermediate. The RNA binding domain of heterogeneous nuclear ribonucleoprotein A1 protein, a structurally unrelated chaperone, also accelerated dimerization. Both chaperones interacted primarily with guanosine residues. Replacing guanosine with more weakly pairing inosine yielded an RNA that folded rapidly without a facilitating chaperone. These results show that RNA chaperones can simplify RNA folding landscapes by weakening intramolecular interactions involving guanosine and explain many RNA chaperone activities.
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.