Evidence map›Paper›PMID 11233973›Full record

ArticleRNA (New York, N.Y.)2001

An early transition state for folding of the P4-P6 RNA domain.

S K Silverman, T R Cech

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 64 citations in OpenAlex.

  1. Rho (bioRxiv : the preprint server for biology · 2026
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  12. Entropic origin of Mg2+-facilitated RNA folding.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Article
  14. Hinge stiffness is a barrier to RNA folding.Journal of molecular biology · 2008
    Article
  15. Article
  16. Article
  17. Article
  18. Single-molecule transition-state analysis of RNA folding.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  19. RNA hairpin-folding kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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

2 authors at 2 institutions in 1 country.

S K SilvermanDepartment of Chemistry and Biochemistry, University of Colorado at Boulder, 80309-0215, USA. scott@scs.uiuc.edu
T R Cech
University of Colorado Boulder · USUniversity of Illinois Urbana-Champaign · US

Funding

Telomerase and Telomeres: Structure, Function/RegulationR01GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS ROBERT · 1985 to 2009
$2.6M
STUDIES OF NUCLEIC ACID STRUCTURE AND REACTIVITYR37GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS R · 1988 to 1997
–
NIGMS NIH HHS GM28039
6 · The paper itself

Abstract

Tertiary folding of the 160-nt P4-P6 domain of the Tetrahymena group I intron RNA involves burying of substantial surface area, providing a model for the folding of other large RNA domains involved in catalysis. Stopped-flow fluorescence was used to monitor the Mg2+-induced tertiary folding of pyrene-labeled P4-P6. At 35 degrees C with [Mg2+] approximately 10 mM, P4-P6 folds on the tens of milliseconds timescale with k(obs) = 15-31 s(-1). From these values, an activation free energy deltaG(double dagger) of approximately 8-16 kcal/mol is calculated, where the large range for deltaG(double dagger) arises from uncertainty in the pre-exponential factor relating k(obs) and delta G(double dagger). The folding rates of six mutant P4-P6 RNAs were measured and found to be similar to that of the wild-type RNA, in spite of significant thermodynamic destabilization or stabilization. The ratios of the kinetic and thermodynamic free energy changes phi = delta deltaG(double dagger)/delta deltaG(o') are approximately 0, implying a folding transition state in which most of the native-state tertiary contacts are not yet formed (an early folding transition state). The k(obs) depends on the Mg2+ concentration, and the initial slope of k(obs) versus [Mg2+] suggests that only approximately 1 Mg2+ ion is bound in the rate-limiting folding step. This is consistent with an early folding transition state, because folded P4-P6 binds many Mg2+ ions. The observation of a substantial deltaG(double dagger) despite an early folding transition state suggests that a simple two-state folding diagram for Mg2+-induced P4-P6 folding is incomplete. Our kinetic data are some of the first to provide quantitative values for an activation barrier and location of a transition state for tertiary folding of an RNA domain.

Indexed as

Nucleic Acid ConformationAnimalsKineticsMagnesiumMutationPyrenesRNARNA, CatalyticRNA, ProtozoanSpectrometry, FluorescenceTetrahymenaThermodynamicsMagnesiumPyrenesRNARNA, CatalyticRNA, Protozoan

Identifiers

PMID11233973
PMCPMC1370074
OpenAlexW2110790388

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.