Evidence map›Paper›PMID 32164257›Full record

ArticleBiomolecules2020

Codon Harmonization of a Kir3.1-KirBac1.3 Chimera for Structural Study Optimization.

Evan van Aalst, Maryam Yekefallah, Anil K Mehta, Isaac Eason, Benjamin Wylie

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. 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
1.0field-weighted citation impact, top 26% 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, 16 citations in OpenAlex.

  1. Article
  2. Modulation of Aging Diseases via RAGE Targets: A Dietary Intervention Review.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  3. Article
  4. Review
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  6. Article
  7. Spectroscopic signatures of bilayer ordering in native biological membranes.Biochimica et biophysica acta. Biomembranes · 2022
    Article
  8. 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 2 institutions in 1 country.

Evan van AalstDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79423, USA.
Maryam YekefallahDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79423, USA.
Anil K MehtaNational High Magnetic Field Laboratory and McKnight Brain Institute, University of Florida, Box 10015, Gainesville, FL 32610, USA.
Isaac EasonDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79423, USA.
Benjamin WylieDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79423, USA.
Texas Tech University · USUniversity of Florida · US

Funding

The Purchase of a Liquid Chromatography System to facilitate the high-throughput quantification of lipid-protein interactions and membrane ordering using solid-state NMRR35GM124979 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI Benjamin James Wylie · 2017 to 2026
$3.6M
NIGMS NIH HHS R35 GM124979
6 · The paper itself

Abstract

The expression of functional, folded, and isotopically enriched membrane proteins is an enduring bottleneck for nuclear magnetic resonance (NMR) studies. Indeed, historically, protein yield optimization has been insufficient to allow NMR analysis of many complex Eukaryotic membrane proteins. However, recent work has found that manipulation of plasmid codons improves the odds of successful NMR-friendly protein production. In the last decade, numerous studies showed that matching codon usage patterns in recombinant gene sequences to those in the native sequence is positively correlated with increased protein yield. This phenomenon, dubbed codon harmonization, may be a powerful tool in optimizing recombinant expression of difficult-to-produce membrane proteins for structural studies. Here, we apply this technique to an inward rectifier K

Indexed as

G Protein-Coupled Inwardly-Rectifying Potassium ChannelsProtein FoldingRecombinant Fusion ProteinsEscherichia coliHumansNuclear Magnetic Resonance, BiomolecularG Protein-Coupled Inwardly-Rectifying Potassium ChannelsRecombinant Fusion Proteinscodon biascodon harmonizationK+ channelsnuclear magnetic resonance (NMR)protein expressionprotein folding

Identifiers

PMID32164257
PMCPMC7175280
OpenAlexW3011059722

What OpenQuestion holds

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LicenceCC BY
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.