Evidence map›Paper›PMID 24769285›Full record

ReviewBiochimica et biophysica acta2014

Global analysis of riboswitches by small-angle X-ray scattering and calorimetry.

Jinwei Zhang, Christopher P Jones, Adrian R Ferré-D'Amaré

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Biomolecules · 2024
    Article
  4. Article
  5. Article
  6. Getting to the bottom of lncRNA mechanism: structure-function relationships.Mammalian genome : official journal of the International Mammalian Genome Society · 2022
    Review
  7. The roles of structural dynamics in the cellular functions of RNAs.Nature reviews. Molecular cell biology · 2019
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Enthalpy-entropy compensation: the role of solvation.European biophysics journal : EBJ · 2017
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Jinwei ZhangNational Heart, Lung and Blood Institute, 50 South Drive, MSC 8012, Bethesda, MD, 20892-8012, USA.
Christopher P JonesNational Heart, Lung and Blood Institute, 50 South Drive, MSC 8012, Bethesda, MD, 20892-8012, USA.
Adrian R Ferré-D'AmaréNational Heart, Lung and Blood Institute, 50 South Drive, MSC 8012, Bethesda, MD, 20892-8012, USA. Electronic address: adrian.ferre@nih.gov.
National Heart Lung and Blood Institute · US

Funding

RNA: Structure, Biophysics and PhysiologyZIAHL006102 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FERRÉ-D'AMARÉ, ADRIAN · 2011 to 2025
$14.6M
RNA: New Antimicrobial StrategiesZIAHL006150 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FERRÉ-D'AMARÉ, ADRIAN · 2012 to 2025
$11.8M
Intramural NIH HHS Z99 HL999999Intramural NIH HHS ZIA HL006102Intramural NIH HHS ZIA HL006150
6 · The paper itself

Abstract

Riboswitches are phylogenetically widespread non-coding mRNA domains that directly bind cellular metabolites and regulate transcription, translation, RNA stability or splicing via alternative RNA structures modulated by ligand binding. The details of ligand recognition by many riboswitches have been elucidated using X-ray crystallography and NMR. However, the global dynamics of riboswitch-ligand interactions and their thermodynamic driving forces are less understood. By compiling the work of many laboratories investigating riboswitches using small-angle X-ray scattering (SAXS) and isothermal titration calorimetry (ITC), we uncover general trends and common themes. There is a pressing need for community-wide consensus experimental conditions to allow results of riboswitch studies to be compared rigorously. Nonetheless, our meta-analysis reveals considerable diversity in the extent to which ligand binding reorganizes global riboswitch structures. It also demonstrates a wide spectrum of enthalpy-entropy compensation regimes across riboswitches that bind a diverse set of ligands, giving rise to a relatively narrow range of physiologically relevant free energies and ligand affinities. From the strongly entropy-driven binding of glycine to the predominantly enthalpy-driven binding of c-di-GMP to their respective riboswitches, these distinct thermodynamic signatures reflect the versatile strategies employed by RNA to adapt to the chemical natures of diverse ligands. Riboswitches have evolved to use a combination of long-range tertiary interactions, conformational selection, and induced fit to work with distinct ligand structure, charge, and solvation properties. This article is part of a Special Issue entitled: Riboswitches.

Indexed as

Conformational selectionEnthalpy–entropy compensationInduced fitIsothermal titration calorimetrySmall-angle X-ray scattering

Identifiers

PMID24769285
PMCPMC4177933
OpenAlexW2024947747

What OpenQuestion holds

Textmetadata
LicenceTDM
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.