Evidence map›Paper›PMID 27318814›Full record

ReviewCurrent opinion in structural biology2016

Quality over quantity: optimizing co-translational protein folding with non-'optimal' synonymous codons.

Giselle N Jacobson, Patricia L Clark

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.1field-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

37 citing papers in PubMed, 73 citations in OpenAlex.

  1. Modifications of the 5' region of the CASPONMicrobial cell factories · 2024
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Network analysis of synonymous codon usage.Bioinformatics (Oxford, England) · 2020
    Article
  11. Article
  12. Article
  13. Synonymous codon substitutions perturb cotranslational protein folding in vivo and impair cell fitness.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Evidence of multifaceted functions of codon usage in translation within the model beetle Tribolium castaneum.DNA research : an international journal for rapid publication of reports on genes and genomes · 2019
    Article
  17. Article
  18. Review
  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

2 authors at 1 institution in 1 country.

Giselle N JacobsonDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Patricia L ClarkDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA; Department of Chemical & Biomolecular Engineering, University of Notre Dame, Notre Dame, IN 46556, USA. Electronic address: pclark1@nd.edu.
University of Notre Dame · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
Influence of Translation on Protein FoldingR01GM074807 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2005 to 2014
$2.8M
OUTER MEMBRANE SECRETION MECHANISM FOR AUTOTRANSPORTER PROTEINSR01GM097573 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM074807NIGMS NIH HHS R01 GM097573NIGMS NIH HHS T32 GM075762NIGMS NIH HHS U54 GM105816
6 · The paper itself

Abstract

Protein folding occurs on a time scale similar to peptide bond formation by the ribosome, which has long sparked speculation that altering translation rate could alter the folding mechanism or even the final folded structure of a protein in vivo. Recent results have provided strong support for this model: synonymous substitutions to codons with different usage frequency, which are often translated at different rates, have been shown to significantly alter the co-translational folding mechanism of some proteins, leading to altered cell function. Here we review recent progress towards understanding the connections between synonymous codon usage, translation rate and co-translational protein folding mechanisms.

Indexed as

Protein BiosynthesisProtein FoldingCodonHumansProteinsRibosomesCodonProteins

Identifiers

PMID27318814
PMCPMC5010456
OpenAlexW2433535207

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.