Evidence map›Paper›PMID 24570483›Full record

ArticleRNA (New York, N.Y.)2014

Principles of ion recognition in RNA: insights from the group II intron structures.

Marco Marcia, Anna Marie Pyle

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Controlled dynamic remodeling of the spliceosome active site enables the first step of splicing.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  17. Nucleobase carbonyl groups are poor MgRNA (New York, N.Y.) · 2019
    Article
  18. Optimal molecular crowding accelerates group II intron folding and maximizes catalysis.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

2 authors at 2 institutions in 1 country.

Marco Marcia
Anna Marie Pyle
Howard Hughes Medical Institute · USYale University · US

Funding

STUCTURE AND FUNCTION OF GROUP II INTRONSR01GM050313 · NIGMS · YALE UNIVERSITY · PI PYLE, ANNA MARIE · 1994 to 2016
$4.6M
NIGMS NIH HHS R01 GM050313NIGMS NIH HHS R01GM50313
6 · The paper itself

Abstract

Metal ions promote both RNA folding and catalysis, thus being essential in stabilizing the structure and determining the function of large RNA molecules, including group II introns. The latter are self-splicing metalloribozymes, containing a heteronuclear four-metal-ion center within the active site. In addition to these catalytic ions, group II introns bind many other structural ions, including delocalized ions that bind the RNA diffusively and well-ordered ions that bind the RNA tightly with high occupancy. The latter ions, which can be studied by biophysical methods, have not yet been analyzed systematically. Here, we compare crystal structures of the group IIC intron from Oceanobacillus iheyensis and classify numerous site-bound ions, which are primarily localized in the intron core and near long-range tertiary contacts. Certain ion-binding sites resemble motifs observed in known RNA structures, while others are idiosyncratic to the group II intron. Particularly interesting are (1) ions proximal to the active site, which may participate in splicing together with the catalytic four-metal-ion center, (2) organic ions that bind regions predicted to interact with intron-encoded proteins, and (3) unusual monovalent ions bound to GU wobble pairs, GA mismatches, the S-turn, the tetraloop-receptor, and the T-loop. Our analysis extends the general principles by which ions participate in RNA structural organization and it will aid in the determination and interpretation of future RNA structures.

Indexed as

BacillalesBinding SitesCatalytic DomainIntronsMetalsModels, MolecularNucleic Acid ConformationProtein ConformationRNA, BacterialRNA-Binding ProteinsRNA, CatalyticRNA SplicingMetalsRNA, BacterialRNA-Binding ProteinsRNA, CatalyticGA imino mismatchribonucleoproteinsplicingtetraloop-receptorT-loopX-ray crystallography

Identifiers

PMID24570483
PMCPMC3964913
OpenAlexW2041304468

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.