Evidence map›Paper›PMID 34971617›Full record

ArticleBiophysical journal2022

Hidden intermediates in Mango III RNA aptamer folding revealed by pressure perturbation.

Balasubramanian Harish, Jinqiu Wang, Eric J Hayden, Bastian Grabe, Wolf Hiller, Roland Winter, Catherine A Royer

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Folding and unfolding dynamics of a DNA aptamer studied by heteronuclearJournal of magnetic resonance (San Diego, Calif. : 1997) · 2026
    Article
  2. Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Pressure pushes tRNAProceedings of the National Academy of Sciences of the United States of America · 2023
    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

7 authors at 3 institutions in 2 countries.

Balasubramanian HarishDepartment of Biological Sciences, Rensselaer Polytechnic Institute, Troy.
Jinqiu WangDepartment of Biological Sciences, Rensselaer Polytechnic Institute, Troy.
Eric J HaydenDepartment of Biology, Boise State University, Boise.
Bastian GrabeDepartment of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Wolf HillerDepartment of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Roland WinterPhysical Chemistry I - Biophysical Chemistry, Department of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Catherine A RoyerDepartment of Biological Sciences, Rensselaer Polytechnic Institute, Troy. Electronic address: royerc@rpi.edu.
Rensselaer Polytechnic Institute · USTU Dortmund University · DEBoise State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent RNA aptamers have the potential to enable routine quantitation and localization of RNA molecules and serve as models for understanding biologically active aptamers. In recent years, several fluorescent aptamers have been selected and modified to improve their properties, revealing that small changes to the RNA or the ligands can modify significantly their fluorescent properties. Although structural biology approaches have revealed the bound, ground state of several fluorescent aptamers, characterization of low-abundance, excited states in these systems is crucial to understanding their folding pathways. Here we use pressure as an alternative variable to probe the suboptimal states of the Mango III aptamer with both fluorescence and NMR spectroscopy approaches. At moderate KCl concentrations, increasing pressure disrupted the G-quadruplex structure of the Mango III RNA and led to an intermediate with lower fluorescence. These observations indicate the existence of suboptimal RNA structural states that still bind the TO1-biotin fluorophore and moderately enhance fluorescence. At higher KCl concentration as well, the intermediate fluorescence state was populated at high pressure, but the G-quadruplex remained stable at high pressure, supporting the notion of parallel folding and/or binding pathways. These results demonstrate the usefulness of pressure for characterizing RNA folding intermediates.

Indexed as

Aptamers, NucleotideMangiferaFluorescent DyesRNARNA FoldingAptamers, NucleotideFluorescent DyesRNA

Identifiers

PMID34971617
PMCPMC8822612
OpenAlexW4200595955

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.