Evidence map›Paper›PMID 33877605›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Gel-Based Analysis of Protein-Nucleic Acid Interactions.

James A W Stowell, Terence T L Tang, Maximilian Seidel, Lori A Passmore

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Biophysical Characterization of the MMethods in molecular biology (Clifton, N.J.) · 2025
    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 1 country.

James A W StowellMRC Laboratory of Molecular Biology, Cambridge, UK.
Terence T L TangMRC Laboratory of Molecular Biology, Cambridge, UK.
Maximilian SeidelMRC Laboratory of Molecular Biology, Cambridge, UK.
Lori A PassmoreMRC Laboratory of Molecular Biology, Cambridge, UK. passmore@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105192715
6 · The paper itself

Abstract

Electrophoretic mobility shift assays (EMSAs) are among the most frequently used and straightforward experiments for studying protein-nucleic acid interactions. EMSAs rely on the principle that protein-nucleic acid complexes have reduced electrophoretic mobility in a native gel matrix compared to free nucleic acid due to their larger size and reduced negative charge. Therefore, bands for the protein-nucleic acid complexes are shifted in a gel and can be distinguished from free nucleic acids. EMSAs remain a popular technique since they do not require specialist equipment and the complexes formed are easily visualized. Furthermore, the technique can be adapted to enable various aspects of protein-nucleic acid interactions to be investigated, including sequence specificity, estimated binding affinity, and binding stoichiometry.

Indexed as

Acrylic ResinsBiophysical PhenomenaDNAElectrophoretic Mobility Shift AssayNucleic AcidsProtein BindingProteinsRNAAcrylic ResinsDNANucleic Acidspolyacrylamide gelsProteinsRNAAffinity measurementBand shift assayElectrophoretic mobility shift assayEMSAProtein–DNA interactionsProtein–RNA interactions

Identifiers

PMID33877605
PMCPMC7614308
OpenAlexW3152847180

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.