Evidence map›Paper›PMID 27495142›Full record

ArticleAnalytical biochemistry2016

Rapid agarose gel electrophoretic mobility shift assay for quantitating protein: RNA interactions.

Jennifer A Ream, L Kevin Lewis, Karen A Lewis

Abstract read
In one paragraph

Article in Analytical biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

38 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. S267P mutation of OxyR regulator inSynthetic and systems biotechnology · 2026
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  3. Microbiology spectrum · 2026
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  7. Tandem ssDNA in neutrophil extracellular traps binds thrombin and regulates immunothrombosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  11. Article
  12. Article
  13. Article
  14. Discovery of novel disease-causing mutation inMolecular therapy. Nucleic acids · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Jennifer A ReamDepartment of Chemistry and Biochemistry, Texas State University, 601 University Dr., San Marcos, TX, 78666, USA.
L Kevin LewisDepartment of Chemistry and Biochemistry, Texas State University, 601 University Dr., San Marcos, TX, 78666, USA.
Karen A LewisDepartment of Chemistry and Biochemistry, Texas State University, 601 University Dr., San Marcos, TX, 78666, USA. Electronic address: karen.lewis@txstate.edu.
Texas State University · US

Funding

Molecular Mechanisms of the Posttranscriptional Regulator LARP6R15GM119096 · NIGMS · TEXAS STATE UNIVERSITY · PI LEWIS, KAREN ADELL · 2016 to 2019
$891k
Genome-wide analysis identifies genes required for repair of DNA strand breaksR15GM099049 · NIGMS · TEXAS STATE UNIVERSITY · PI LEWIS, LYSLE KEVIN · 2012 to 2012
$293k
NIGMS NIH HHS R15 GM099049NIGMS NIH HHS R15 GM119096
6 · The paper itself

Abstract

Interactions between proteins and nucleic acids are frequently analyzed using electrophoretic mobility shift assays (EMSAs). This technique separates bound protein:nucleic acid complexes from free nucleic acids by electrophoresis, most commonly using polyacrylamide gels. The current study utilizes recent advances in agarose gel electrophoresis technology to develop a new EMSA protocol that is simpler and faster than traditional polyacrylamide methods. Agarose gels are normally run at low voltages (∼10 V/cm) to minimize heating and gel artifacts. In this study we demonstrate that EMSAs performed using agarose gels can be run at high voltages (≥20 V/cm) with 0.5 × TB (Tris-borate) buffer, allowing for short run times while simultaneously yielding high band resolution. Several parameters affecting band and image quality were optimized for the procedure, including gel thickness, agarose percentage, and applied voltage. Association of the siRNA-binding protein p19 with its target RNA was investigated using the new system. The agarose gel and conventional polyacrylamide gel methods generated similar apparent binding constants in side-by-side experiments. A particular advantage of the new approach described here is that the short run times (5-10 min) reduce opportunities for dissociation of bound complexes, an important concern in non-equilibrium nucleic acid binding experiments.

Indexed as

Electrophoresis, Agar GelElectrophoretic Mobility Shift AssayRNARNA-Binding ProteinsRNARNA-Binding ProteinsBinding affinityDNA bindingElectrophoretic mobility shift assayGel shift assayNucleic acid binding proteinRNA binding

Identifiers

PMID27495142
PMCPMC5002362
OpenAlexW2506013064

What OpenQuestion holds

Textmetadata
LicenceTDM
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.