Evidence map›Paper›PMID 19095619›Full record

ArticleRNA (New York, N.Y.)2009

Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA.

Alexei V Kazantsev, Angelika A Krivenko, Norman R Pace

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Coevolution of RNase P and the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  2. Article
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  12. Time-Resolved, Single-Molecule, Correlated Chemical Probing of RNA.Journal of the American Chemical Society · 2020
    Article
  13. Nucleobase carbonyl groups are poor MgRNA (New York, N.Y.) · 2019
    Article
  14. Article
  15. Article
  16. TheJournal of bacteriology · 2017
    Article
  17. Review
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  19. Review
  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

3 authors.

Alexei V KazantsevDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado at Boulder, 80309, USA.
Angelika A Krivenko
Norman R Pace

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribonuclease P (RNase P) is a ribonucleoprotein enzyme that contains a universally conserved, catalytically active RNA component. RNase P RNA requires divalent metal ions for folding, substrate binding, and catalysis. Despite recent advances in understanding the structure of RNase P RNA, no comprehensive analysis of metal-binding sites has been reported, in part due to the poor crystallization properties of this large RNA. We have developed an abbreviated yet still catalytic construct, Bst P7Delta RNA, which contains the catalytic domain of the bacterial RNase P RNA and has improved crystallization properties. We use this mutant RNA as well as the native RNA to map metal-binding sites in the catalytic core of the bacterial RNase P RNA, by anomalous scattering in diffraction analysis. The results provide insight into the interplay between RNA structure and focalization of metal ions, and a structural basis for some previous biochemical observations with RNase P. We use electrostatic calculations to extract the potential functional significance of these metal-binding sites with respect to binding Mg(2+). The results suggest that with at least one important exception of specific binding, these sites mainly map areas of diffuse association of magnesium ions.

Indexed as

Binding SitesCatalysisCrystallography, X-RayGeobacillus stearothermophilusMagnesiumNucleic Acid ConformationRibonuclease PRNA, BacterialMagnesiumRibonuclease PRNA, Bacterial

Identifiers

PMID19095619
PMCPMC2648716

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.