Evidence map›Paper›PMID 28446709›Full record

ReviewOpen biology2017

Control of mitochondrial biogenesis and function by the ubiquitin-proteasome system.

Piotr Bragoszewski, Michal Turek, Agnieszka Chacinska

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

116 citing papers in PubMed, 189 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mitochondrial proteostasis regulated by CRL5Communications biology · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

56 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

3 authors at 1 institution in 1 country.

Piotr BragoszewskiLaboratory of Mitochondrial Biogenesis, International Institute of Molecular and Cell Biology, Ks. Trojdena 4, 02-109 Warsaw, Poland pbragoszewski@iimcb.gov.pl.
Michal TurekLaboratory of Mitochondrial Biogenesis, International Institute of Molecular and Cell Biology, Ks. Trojdena 4, 02-109 Warsaw, Poland.
Agnieszka ChacinskaLaboratory of Mitochondrial Biogenesis, International Institute of Molecular and Cell Biology, Ks. Trojdena 4, 02-109 Warsaw, Poland a.chacinska@cent.uw.edu.pl.ORCID 0000-0002-2832-2568
International Institute of Molecular and Cell Biology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are pivotal organelles in eukaryotic cells. The complex proteome of mitochondria comprises proteins that are encoded by nuclear and mitochondrial genomes. The biogenesis of mitochondrial proteins requires their transport in an unfolded state with a high risk of misfolding. The mislocalization of mitochondrial proteins is deleterious to the cell. The electron transport chain in mitochondria is a source of reactive oxygen species that damage proteins. Mitochondrial dysfunction is linked to many pathological conditions and, together with the loss of cellular protein homeostasis (proteostasis), are hallmarks of ageing and ageing-related degeneration diseases. The pathogenesis of neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease, has been associated with mitochondrial and proteostasis failure. Thus, mitochondrial proteins require sophisticated surveillance mechanisms. Although mitochondria form a proteasome-exclusive compartment, multiple lines of evidence indicate a crucial role for the cytosolic ubiquitin-proteasome system (UPS) in the quality control of mitochondrial proteins. The proteasome affects mitochondrial proteins at stages of their biogenesis and maturity. The effects of the UPS go beyond the removal of damaged proteins and include the adjustment of mitochondrial proteome composition, the regulation of organelle dynamics and the protection of cellular homeostasis against mitochondrial failure. In turn, mitochondrial activity and mitochondrial dysfunction adjust the activity of the UPS, with implications at the cellular level.

Indexed as

HumansMitochondriaMitochondrial DynamicsMitochondrial ProteinsMitophagyNeurodegenerative DiseasesProteasome Endopeptidase ComplexProtein KinasesPTEN-Induced Putative KinaseUbiquitinUbiquitin-Protein LigasesMitochondrial Proteinsparkin proteinProteasome Endopeptidase ComplexProtein KinasesPTEN-Induced Putative KinaseUbiquitinUbiquitin-Protein Ligasesmitochondriaproteasomeprotein biogenesisproteostasisubiquitinubiquitin–proteasome system

Identifiers

PMID28446709
PMCPMC5413908
OpenAlexW2608366497

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.