Evidence map›Paper›PMID 26590636›Full record

ArticleChemistry & biology2015

An L-RNA Aptamer that Binds and Inhibits RNase.

Charles Olea, Joachim Weidmann, Philip E Dawson, Gerald F Joyce

Abstract read
In one paragraph

Article in Chemistry & biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Spiegelmer-Based Sandwich Assay for Cardiac Troponin I Detection.International journal of molecular sciences · 2020
    Article
  12. Mirror-Image Oligonucleotides: History and Emerging Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019
    Review
  13. Article
  14. Article
  15. Selection of DNA aptamers with two modified bases.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

4 authors at 1 institution in 2 countries.

Charles OleaDepartment of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Joachim WeidmannDepartment of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Division of Functional Genome Analysis, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 580, 69120 Heidelberg, Germany.
Philip E DawsonDepartment of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Gerald F JoyceDepartment of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: gjoyce@scripps.edu.
Scripps Research Institute · US

Funding

Ligand-Dependent Exponential Amplification of RNAR01GM065130 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI JOYCE, GERALD F · 2002 to 2015
$4.1M
Real-time detection of cancer biomarkers using a self-sustained aptazymeF32CA165430 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI OLEA, CHARLES · 2011 to 2013
$155k
NCI NIH HHS F32 CA165430NCI NIH HHS F32CA165430NIGMS NIH HHS GM065130NIGMS NIH HHS R01 GM065130
6 · The paper itself

Abstract

L-RNA aptamers were developed that bind to barnase RNase and thereby inhibit the function of the enzyme. These aptamers were obtained by first carrying out in vitro selection of D-RNAs that bind to the full-length synthetic D-enantiomer of barnase, then reversing the mirror and preparing L-RNAs of identical sequence that similarly bind to natural L-barnase. The resulting L-aptamers bind L-barnase with an affinity of ∼100 nM and function as competitive inhibitors of enzyme cleavage of D-RNA substrates. L-RNA aptamers are resistant to degradation by ribonucleases, thus enabling them to function in biological samples, most notably for applications in molecular diagnostics and therapeutics. In addition to the irony of using RNA to inhibit RNase, L-RNA aptamers such as those described here could be used to measure the concentration or inhibit the function of RNase in the laboratory or in biological systems.

Indexed as

Aptamers, NucleotideBacterial ProteinsBase SequenceBinding, CompetitiveBinding SitesMolecular Sequence DataMutagenesis, Site-DirectedNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRibonucleasesRNASubstrate SpecificityAptamers, NucleotideBacillus amyloliquefaciens ribonucleaseBacterial ProteinsDNA-like RNARibonucleasesRNA

Identifiers

PMID26590636
PMCPMC4656138
OpenAlexW2176054603

What OpenQuestion holds

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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.