Evidence map›Paper›PMID 22219369›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Folding energy landscape of the thiamine pyrophosphate riboswitch aptamer.

Peter C Anthony, Christian F Perez, Cuauhtémoc García-García, Steven M Block

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
–field-weighted citation impact
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

42 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Roquin exhibits opposing effects on RNA stem-loop stability through its two ROQ domain binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Monitoring RNA dynamics in native transcriptional complexes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Alternate RNA Structures.Cold Spring Harbor perspectives in biology · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Self-cleavage of theProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Single-molecule FRET studies on the cotranscriptional folding of a thiamine pyrophosphate riboswitch.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Review
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

4 authors.

Peter C AnthonyBiophysics Program, Department of Physics, Stanford University, Stanford, CA 94305, USA.
Christian F Perez
Cuauhtémoc García-García
Steven M Block

Funding

Nucleic Acid Enzymes and Nucleic Acids Studied at the Molecular LevelR37GM057035 · NIGMS · STANFORD UNIVERSITY · PI BLOCK, STEVEN M · 2010 to 2019
$5.7M
NIGMS NIH HHS R37 GM057035
6 · The paper itself

Abstract

Riboswitches are motifs in the untranslated regions (UTRs) of RNA transcripts that sense metabolite levels and modulate the expression of the corresponding genes for metabolite import, export, synthesis, or degradation. All riboswitches contain an aptamer: an RNA structure that, upon binding ligand, folds to expose or sequester regulatory elements in the adjacent sequence through alternative nucleotide pairing. The coupling between ligand binding and aptamer folding is central to the regulatory mechanisms of thiamine pyrophosphate (TPP) riboswitches and has not been fully characterized. Here, we show that TPP aptamer folding can be decomposed into ligand-independent and -dependent steps that correspond to the formation of secondary and tertiary structures, respectively. We reconstructed the full energy landscape for folding of the wild-type (WT) aptamer and measured perturbations of this landscape arising from mutations or ligand binding. We show that TPP binding proceeds in two steps, from a weakly to a strongly bound state. Our data imply a hierarchical folding sequence, and provide a framework for understanding molecular mechanism throughout the TPP riboswitch family.

Indexed as

Nucleic Acid ConformationRiboswitchAptamers, NucleotideBase SequenceKineticsMolecular Sequence DataThiamine PyrophosphateAptamers, NucleotideRiboswitchThiamine Pyrophosphate

Identifiers

PMID22219369
PMCPMC3277107

What OpenQuestion holds

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Registered trials

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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.