Evidence map›Paper›PMID 38134335›Full record

ReviewAnnual review of biophysics2024

The Effects of Codon Usage on Protein Structure and Folding.

McKenze J Moss, Laura M Chamness, Patricia L Clark

Open access · hybridAbstract readReview
In one paragraph

Review in Annual review of biophysics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
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  4. Article
  5. NNature · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Analysis of Codon Usage Bias in theThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2026
    Article
  13. Review
  14. Article
  15. Review
  16. Article
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  18. Review
  19. Identification of an on-pathway intermediate illuminates the kinetic competition between protein folding and misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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.

McKenze J MossDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA; email: mmoss6@nd.edu, lchamnes@nd.edu, pclark1@nd.edu.
Laura M ChamnessDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA; email: mmoss6@nd.edu, lchamnes@nd.edu, pclark1@nd.edu.
Patricia L ClarkDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA; email: mmoss6@nd.edu, lchamnes@nd.edu, pclark1@nd.edu.
University of Notre Dame · US

Funding

Decoding the regulation of protein folding by synonymous codon usageDP1GM146256 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2021 to 2025
$5.5M
NIGMS NIH HHS DP1 GM146256
6 · The paper itself

Abstract

The rate of protein synthesis is slower than many folding reactions and varies depending on the synonymous codons encoding the protein sequence. Synonymous codon substitutions thus have the potential to regulate cotranslational protein folding mechanisms, and a growing number of proteins have been identified with folding mechanisms sensitive to codon usage. Typically, these proteins have complex folding pathways and kinetically stable native structures. Kinetically stable proteins may fold only once over their lifetime, and thus, codon-mediated regulation of the pioneer round of protein folding can have a lasting impact. Supporting an important role for codon usage in folding, conserved patterns of codon usage appear in homologous gene families, hinting at selection. Despite these exciting developments, there remains few experimental methods capable of quantifying translation elongation rates and cotranslational folding mechanisms in the cell, which challenges the development of a predictive understanding of how biology uses codons to regulate protein folding.

Indexed as

CodonProtein FoldingProteinsAnimalsCodon UsageHumansProtein BiosynthesisProtein ConformationCodonProteinscotranslational protein foldingfunctional protein productiongene expressionrare codonssynonymous codon substitutiontranslation elongation

Identifiers

PMID38134335
PMCPMC11227313
OpenAlexW4390098716

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.