Evidence map›Paper›PMID 26030272›Full record

ReviewCell cycle (Georgetown, Tex.)2015

Mitochondrial ribosome assembly in health and disease.

Dasmanthie De Silva, Ya-Ting Tu, Alexey Amunts, Flavia Fontanesi, Antoni Barrientos

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

121 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. Article
  8. Human lncRNAProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Article
  10. Article
  11. Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Mitochondrial Ribosomal Proteins and Cancer.Medicina (Kaunas, Lithuania) · 2025
    Review
  20. Article

61 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 2 countries.

Dasmanthie De Silvaa Department of Biochemistry and Molecular Biology ; University of Miami Miller School of Medicine ; Miami , FL USA.
Ya-Ting Tu
Alexey Amunts
Flavia Fontanesi
Antoni Barrientos
University of Miami · USMedical Research Council · GB

Funding

CYTOCHROME C OXIDASE IN HEALTH AND DISEASER01GM071775 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2006 to 2015
$3.1M
The Biosynthetic Pathway of Mitochondrial RespirasomesR01GM105781 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2014 to 2016
$894k
Biogenesis of the Mitochondrial Translation MachineryR01GM112179 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2015 to 2016
$584k
NIGMS NIH HHS GM105781NIGMS NIH HHS GM112179NIGMS NIH HHS R01 GM071775NIGMS NIH HHS R01 GM112179
6 · The paper itself

Abstract

The ribosome is a structurally and functionally conserved macromolecular machine universally responsible for catalyzing protein synthesis. Within eukaryotic cells, mitochondria contain their own ribosomes (mitoribosomes), which synthesize a handful of proteins, all essential for the biogenesis of the oxidative phosphorylation system. High-resolution cryo-EM structures of the yeast, porcine and human mitoribosomal subunits and of the entire human mitoribosome have uncovered a wealth of new information to illustrate their evolutionary divergence from their bacterial ancestors and their adaptation to synthesis of highly hydrophobic membrane proteins. With such structural data becoming available, one of the most important remaining questions is that of the mitoribosome assembly pathway and factors involved. The regulation of mitoribosome biogenesis is paramount to mitochondrial respiration, and thus to cell viability, growth and differentiation. Moreover, mutations affecting the rRNA and protein components produce severe human mitochondrial disorders. Despite its biological and biomedical significance, knowledge on mitoribosome biogenesis and its deviations from the much-studied bacterial ribosome assembly processes is scarce, especially the order of rRNA processing and assembly events and the regulatory factors required to achieve fully functional particles. This article focuses on summarizing the current available information on mitoribosome assembly pathway, factors that form the mitoribosome assembly machinery, and the effect of defective mitoribosome assembly on human health.

Indexed as

GTP PhosphohydrolasesHumansMicroRNAsMitochondrial DiseasesMitochondrial RibosomesProtein Structure, QuaternaryRNA HelicasesRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsGTP PhosphohydrolasesMicroRNAsRNA HelicasesRNA, RibosomalSaccharomyces cerevisiae ProteinsTrans-Activatorsmitochondrial diseasemitochondrial ribosomemitochondrial translationmitochondriolusmitoribosome assemblymitoribosome assembly factormitoribosome biogenesis

Identifiers

PMID26030272
PMCPMC4615001
OpenAlexW1614372115

What OpenQuestion holds

Textmetadata
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.