Evidence map›Paper›PMID 18429611›Full record

ArticleJournal of the American Chemical Society2008

Direct measurement of tertiary contact cooperativity in RNA folding.

Bernie D Sattin, Wei Zhao, Kevin Travers, Steven Chu, Daniel Herschlag

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Dissecting the energetic architecture within an RNA tertiary structural motif via high-throughput thermodynamic measurements.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Cooperativity and Allostery in RNA Systems.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  6. Review
  7. Review
  8. Article
  9. Quantitative tests of a reconstitution model for RNA folding thermodynamics and kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Article
  20. Understanding nucleic acid-ion interactions.Annual review of biochemistry · 2014
    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

5 authors.

Bernie D SattinDepartment of Biochemistry, Stanford University, Stanford, California 94305, USA.
Wei Zhao
Kevin Travers
Steven Chu
Daniel Herschlag

Funding

Time-resolved small angle X-ray scatteringP01GM066275 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2003 to 2017
$17.8M
Quantitative Chemical Biology(RMI)R90DK071499 · NIDDK · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 2004 to 2008
$1.1M
NIDDK NIH HHS DK071499NIDDK NIH HHS R90 DK071499NIGMS NIH HHS P01 GM066275NIGMS NIH HHS P01-GM-066275
6 · The paper itself

Abstract

All structured biological macromolecules must overcome the thermodynamic folding problem to populate a unique functional state among a vast ensemble of unfolded and alternate conformations. The exploration of cooperativity in protein folding has helped reveal and distinguish the underlying mechanistic solutions to this folding problem. Analogous dissections of RNA tertiary stability remain elusive, however, despite the central biological importance of folded RNA molecules and the potential to reveal fundamental properties of structured macromolecules via comparisons of protein and RNA folding. We report a direct quantitative measure of tertiary contact cooperativity in a folded RNA. We precisely measured the stability of an independently folding P4-P6 domain from the Tetrahymena thermophila group I intron by single molecule fluorescence resonance energy transfer (smFRET). Using wild-type and mutant RNAs, we found that cooperativity between the two tertiary contacts enhances P4-P6 stability by 3.2 +/- 0.2 kcal/mol.

Indexed as

Nucleic Acid ConformationAnimalsBase SequenceFluorescence Resonance Energy TransferKineticsModels, MolecularMolecular Sequence DataRNATetrahymena thermophilaThermodynamicsRNA

Identifiers

PMID18429611
PMCPMC2835547

What OpenQuestion holds

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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.