Evidence map›Paper›PMID 12869691›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Single-molecule transition-state analysis of RNA folding.

Gregory Bokinsky, David Rueda, Vinod K Misra, Maria M Rhodes, Andrew Gordus, Hazen P Babcock, Nils G Walter, Xiaowei Zhuang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing 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

91 citing papers in PubMed.

  1. Article
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  5. Site-Selective RNA Functionalization via DNA-Induced Structure.Journal of the American Chemical Society · 2020
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  18. Molecular crowding accelerates ribozyme docking and catalysis.Journal of the American Chemical Society · 2014
    Article
  19. Review
  20. Article

31 more citing papers are in PubMed but not listed here.

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

8 authors.

Gregory BokinskyDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
David Rueda
Vinod K Misra
Maria M Rhodes
Andrew Gordus
Hazen P Babcock
Nils G Walter
Xiaowei Zhuang

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How RNA molecules fold into functional structures is a problem of great significance given the expanding list of essential cellular RNA enzymes and the increasing number of applications of RNA in biotechnology and medicine. A critical step toward solving the RNA folding problem is the characterization of the associated transition states. This is a challenging task in part because the rugged energy landscape of RNA often leads to the coexistence of multiple distinct structural transitions. Here, we exploit single-molecule fluorescence spectroscopy to follow in real time the equilibrium transitions between conformational states of a model RNA enzyme, the hairpin ribozyme. We clearly distinguish structural transitions between effectively noninterchanging sets of unfolded and folded states and characterize key factors defining the transition state of an elementary folding reaction where the hairpin ribozyme's two helical domains dock to make several tertiary contacts. Our single-molecule experiments in conjunction with site-specific mutations and metal ion titrations show that the two RNA domains are in a contact or close-to-contact configuration in the transition state even though the native tertiary contacts are at most partially formed. Such a compact transition state without well formed tertiary contacts may be a general property of elementary RNA folding reactions.

Indexed as

Nucleic Acid ConformationDose-Response Relationship, DrugKineticsMagnesiumModels, TheoreticalMutationNepovirusPoisson DistributionProtein BindingRNARNA, CatalyticSpectrometry, FluorescenceThermodynamicsUreaMagnesiumRNARNA, CatalyticUrea

Identifiers

PMID12869691
PMCPMC170913

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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.