Evidence map›Paper›PMID 25542647›Full record

ReviewBiochimie2015

Heterogeneity of the translational machinery: Variations on a common theme.

Martina Sauert, Hannes Temmel, Isabella Moll

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimie, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

59 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The ribosomal landscape in influenza A virus infection: from molecular mechanisms to clinical relevance.European respiratory review : an official journal of the European Respiratory Society · 2026
    Review
  9. Ribosomes: from conserved origin to functional/medical mobility and heterogeneity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  10. Article
  11. Intact Mass Proteomics Using a Proteoform Atlas.Journal of proteome research · 2025
    Article
  12. Article
  13. Article
  14. Ribosome Specialization in Protozoa Parasites.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Martina Sauert *Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, Centre for Molecular Biology, University of Vienna, Dr. Bohrgasse 9/4, 1030 Vienna, Austria.
Hannes Temmel *Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, Centre for Molecular Biology, University of Vienna, Dr. Bohrgasse 9/4, 1030 Vienna, Austria.
Isabella MollDepartment of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, Centre for Molecular Biology, University of Vienna, Dr. Bohrgasse 9/4, 1030 Vienna, Austria.
Max Perutz Labs · ATUniversity of Vienna · AT

Funding

Austrian Science Fund FWF F 4316Austrian Science Fund FWF P 20112Austrian Science Fund FWF P 22249Austrian Science Fund FWF P 26946Austrian Science Fund FWF P 27043
6 · The paper itself

Abstract

In all organisms the universal process of protein synthesis is performed by the ribosome, a complex multi-component assembly composed of RNA and protein elements. Although ribosome heterogeneity was observed already more than 40 years ago, the ribosome is still traditionally viewed as an unchangeable entity that has to be equipped with all ribosomal components and translation factors in order to precisely accomplish all steps in protein synthesis. In the recent years this concept was challenged by several studies highlighting a broad variation in the composition of the translational machinery in response to environmental signals, which leads to its adaptation and functional specialization. Here, we summarize recent reports on the variability of the protein synthesis apparatus in diverse organisms and discuss the multiple mechanisms and possibilities that can lead to functional ribosome heterogeneity. Collectively, these results indicate that all cells are equipped with a remarkable toolbox to fine tune gene expression at the level of translation and emphasize the physiological importance of ribosome heterogeneity for the immediate implementation of environmental information.

Indexed as

Protein BiosynthesisAnimalsGene Expression RegulationHumansPeptide Initiation FactorsProtein Processing, Post-TranslationalRibosomal ProteinsRibosomesRNA Processing, Post-TranscriptionalRNA, RibosomalRNA, TransferStress, PhysiologicalPeptide Initiation FactorsRibosomal ProteinsRNA, RibosomalRNA, TransferGene expression regulationProtein synthesisRibosome heterogeneityStress responseTranslation regulation

Identifiers

PMID25542647
PMCPMC4894553
OpenAlexW2035347598

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.