Evidence map›Paper›PMID 38065274›Full record

ReviewJournal of molecular biology2024

Translation Rates and Protein Folding.

Anton A Komar, Ekaterina Samatova, Marina V Rodnina

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Recoding by NNature communications · 2026
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  6. The regulation, function and disease relevance of cytoplasmic tRNAs.Nature reviews. Molecular cell biology · 2026
    Review
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  18. Review
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  20. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    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 2 institutions in 1 country.

Anton A KomarCenter for Gene Regulation in Health and Disease, Department of Biological, Geological and Environmental Sciences, Cleveland State University, 2121 Euclid Avenue, Cleveland, OH 44115, USA; Department of Biochemistry and Center for RNA Science and Therapeutics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. Electronic address: a.komar@csuohio.edu.
Ekaterina SamatovaMax Planck Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, 37077 Goettingen, Germany.
Marina V RodninaMax Planck Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, 37077 Goettingen, Germany. Electronic address: rodnina@mpinat.mpg.de.
Max Planck Institute for Multidisciplinary SciencesCase Western Reserve University · US

Funding

Safer and more effective FIX therapeutics: impact of codon optimizationR01HL151392 · NHLBI · CLEVELAND STATE UNIVERSITY · PI KOMAR, ANTON A. · 2020 to 2023
$1.5M
eIF2A in translational controlR01GM128981 · NIGMS · CLEVELAND STATE UNIVERSITY · PI KOMAR, ANTON A. · 2020 to 2023
$1.2M
NHLBI NIH HHS R01 HL151392NIGMS NIH HHS R01 GM128981
6 · The paper itself

Abstract

The mRNA coding sequence defines not only the amino acid sequence of the protein, but also the speed at which the ribosomes move along the mRNA while making the protein. The non-uniform local kinetics - denoted as translational rhythm - is similar among mRNAs coding for related protein folds. Deviations from this conserved rhythm can result in protein misfolding. In this review we summarize the experimental evidence demonstrating how local translation rates affect cotranslational protein folding, with the focus on the synonymous codons and patches of charged residues in the nascent peptide as best-studied examples. Alterations in nascent protein conformations due to disturbed translational rhythm can persist off the ribosome, as demonstrated by the effects of synonymous codon variants of several disease-related proteins. Charged amino acid patches in nascent chains also modulate translation and cotranslational protein folding, and can abrogate translation when placed at the N-terminus of the nascent peptide. During cotranslational folding, incomplete nascent chains navigate through a unique conformational landscape in which earlier intermediate states become inaccessible as the nascent peptide grows. Precisely tuned local translation rates, as well as interactions with the ribosome, guide the folding pathway towards the native structure, whereas deviations from the natural translation rhythm may favor pathways leading to trapped misfolded states. Deciphering the 'folding code' of the mRNA will contribute to understanding the diseases caused by protein misfolding and to rational protein design.

Indexed as

Protein BiosynthesisProtein FoldingRibosomesAnimalsCodonHumansKineticsProtein ConformationProteinsRNA, MessengerCodonProteinsRNA, Messengercotranslational protein foldingprotein folding energy landscapeprotein misfoldingprotein synthesissynonymous codons

Identifiers

PMID38065274
PMCPMC12262135
OpenAlexW4389366166

What OpenQuestion holds

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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.