Evidence map›Paper›PMID 35408834›Full record

ReviewInternational journal of molecular sciences2022

Types and Functions of Mitoribosome-Specific Ribosomal Proteins across Eukaryotes.

Vassilis Scaltsoyiannes, Nicolas Corre, Florent Waltz, Philippe Giegé

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. RNA regulation in plants.Science China. Life sciences · 2026
    Review
  3. Article
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  15. Article
  16. Research Progress in RNA-Binding Proteins.International journal of molecular sciences · 2022
    Article
  17. 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

4 authors at 1 institution in 2 countries.

Vassilis ScaltsoyiannesCNRS, Institut de Biologie Moléculaire des Plantes, Université de Strasbourg, 67084 Strasbourg, France.ORCID 0000-0003-4155-9540
Nicolas CorreCNRS, Institut de Biologie Moléculaire des Plantes, Université de Strasbourg, 67084 Strasbourg, France.ORCID 0000-0002-4009-7543
Florent WaltzCNRS, Institut de Biologie Moléculaire des Plantes, Université de Strasbourg, 67084 Strasbourg, France.
Philippe GiegéCNRS, Institut de Biologie Moléculaire des Plantes, Université de Strasbourg, 67084 Strasbourg, France.
Centre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche ANR 16 CE11-0024; ANR 20 CE11-0021
6 · The paper itself

Abstract

Mitochondria are key organelles that combine features inherited from their bacterial endosymbiotic ancestor with traits that arose during eukaryote evolution. These energy producing organelles have retained a genome and fully functional gene expression machineries including specific ribosomes. Recent advances in cryo-electron microscopy have enabled the characterization of a fast-growing number of the low abundant membrane-bound mitochondrial ribosomes. Surprisingly, mitoribosomes were found to be extremely diverse both in terms of structure and composition. Still, all of them drastically increased their number of ribosomal proteins. Interestingly, among the more than 130 novel ribosomal proteins identified to date in mitochondria, most of them are composed of a-helices. Many of them belong to the nuclear encoded super family of helical repeat proteins. Here we review the diversity of functions and the mode of action held by the novel mitoribosome proteins and discuss why these proteins that share similar helical folds were independently recruited by mitoribosomes during evolution in independent eukaryote clades.

Indexed as

Mitochondrial RibosomesRibosomal ProteinsCryoelectron MicroscopyEukaryotaMitochondrial ProteinsRNA, RibosomalMitochondrial ProteinsRibosomal ProteinsRNA, Ribosomalhelical repeat proteinsmitochondrial gene expressionpentatricopeptide repeat proteinsribosomessingle particle cryo-EMtranslation

Identifiers

PMID35408834
PMCPMC8998825
OpenAlexW4220652744

What OpenQuestion holds

Textmetadata
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.