Evidence map›Paper›PMID 19946040›Full record

ArticleRNA (New York, N.Y.)2009

A class I ligase ribozyme with reduced Mg2+ dependence: Selection, sequence analysis, and identification of functional tertiary interactions.

Sarah C Bagby, Nicholas H Bergman, David M Shechner, Catherine Yen, David P Bartel

Open access · bronzeAbstract 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Evolution of the substrate specificity of an RNA ligase ribozyme from phosphorimidazole to triphosphate activation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Article
  4. Enhanced group II intron retrohoming in magnesium-deficient Escherichia coli via selection of mutations in the ribozyme core.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  5. Mapping L1 ligase ribozyme conformational switch.Journal of molecular biology · 2012
    Article
  6. Crystal structure of an RNA polymerase ribozyme in complex with an antibody fragment.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011
    Article
  7. The chemical origins of life and its early evolution: an introduction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011
    Article
  8. The structural basis of RNA-catalyzed RNA polymerization.Nature structural & molecular biology · 2011
    Article
  9. Article
  10. Article
  11. 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

5 authors at 1 institution in 1 country.

Sarah C BagbyWhitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142, USA.
Nicholas H Bergman
David M Shechner
Catherine Yen
David P Bartel
Howard Hughes Medical Institute · US

Funding

RNA CONFORMATION AND CATALYSISR01GM061835 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BARTEL, DAVID P · 2000 to 2008
$2.5M
RNA Conformation and CatalysisR37GM061835 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BARTEL, DAVID P · 2011 to 2016
$2.3M
Howard Hughes Medical InstituteNIGMS NIH HHS GM61835NIGMS NIH HHS R01 GM061835NIGMS NIH HHS R37 GM061835
6 · The paper itself

Abstract

The class I ligase was among the first ribozymes to have been isolated from random sequences and represents the catalytic core of several RNA-directed RNA polymerase ribozymes. The ligase is also notable for its catalytic efficiency and structural complexity. Here, we report an improved version of this ribozyme, arising from selection that targeted the kinetics of the chemical step. Compared with the parent ribozyme, the improved ligase achieves a modest increase in rate enhancement under the selective conditions and shows a sharp reduction in [Mg(2+)] dependence. Analysis of the sequences and kinetics of successful clones suggests which mutations play the greatest part in these improvements. Moreover, backbone and nucleobase interference maps of the parent and improved ligase ribozymes complement the newly solved crystal structure of the improved ligase to identify the functionally significant interactions underlying the catalytic ability and structural complexity of the ligase ribozyme.

Indexed as

Protein Interaction Domains and MotifsBase SequenceBinding SitesCrystallography, X-RayGenetic VariationKineticsLigasesMagnesiumModels, MolecularNucleic Acid ConformationRNA, CatalyticSequence Analysis, DNALigasesMagnesiumRNA, Catalytic

Identifiers

PMID19946040
PMCPMC2779684
OpenAlexW2138715324

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.