Evidence map›Paper›PMID 25399908›Full record

ArticleJournal of the American Chemical Society2014

Molecular crowding accelerates ribozyme docking and catalysis.

Bishnu P Paudel, David Rueda

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

49 citing papers in PubMed, 92 citations in OpenAlex.

  1. A passive protein environment offsets RNA folding energetics in cells.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Aggregation of Phosphates Enhances Enzyme Activity in Aqueous Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  4. Article
  5. Reticular Chemistry: A Versatile Platform for Engineering Heterogenous Biocatalysts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Bishnu P PaudelDepartment of Medicine, Section of Virology, and Single Molecule Imaging Group, MRC-Clinical Sciences Centre, Imperial College London , Du Cane Road, London W12 0NN, U.K.
David Rueda
MRC London Institute of Medical Sciences · GB

Funding

Single Molecule Study of Spliceosomal RNAsR01GM085116 · NIGMS · WAYNE STATE UNIVERSITY · PI CHOW, CHRISTINE S · 2008 to 2012
$1.3M
Medical Research Council MC_UP_1102/5Medical Research Council UK, MC_A658_5TY10NIGMS NIH HHS GM085116NIGMS NIH HHS R01 GM085116
6 · The paper itself

Abstract

All biological processes take place in highly crowded cellular environments. However, the effect that molecular crowding agents have on the folding and catalytic properties of RNA molecules remains largely unknown. Here, we have combined single-molecule fluorescence resonance energy transfer (smFRET) and bulk cleavage assays to determine the effect of a molecular crowding agents on the folding and catalysis of a model RNA enzyme, the hairpin ribozyme. Our single-molecule data reveal that PEG favors the formation of the docked (active) structure by increasing the docking rate constant with increasing PEG concentrations. Furthermore, Mg(2+) ion-induced folding in the presence of PEG occurs at concentrations ∼7-fold lower than in the absence of PEG, near the physiological range (∼1 mM). Lastly, bulk cleavage assays in the presence of the crowding agent show that the ribozyme's activity increases while the heterogeneity decreases. Our data is consistent with the idea that molecular crowding plays an important role in the stabilization of ribozyme active conformations in vivo.

Indexed as

Molecular Docking SimulationBiocatalysisFluorescence Resonance Energy TransferMagnesiumPolyethylene GlycolsProtein FoldingProtein StabilityRNA, CatalyticMagnesiumPolyethylene GlycolsRNA, Catalytic

Identifiers

PMID25399908
PMCPMC4277754
OpenAlexW2025696272

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.