Evidence map›Paper›PMID 23508107›Full record

ArticleMolecular and cellular biology2013

The ubiquitin-proteasome system regulates mitochondrial intermembrane space proteins.

Piotr Bragoszewski, Agnieszka Gornicka, Malgorzata E Sztolsztener, Agnieszka Chacinska

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.4field-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

85 citing papers in PubMed, 152 citations in OpenAlex.

  1. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Review
  3. Review
  4. Review
  5. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  6. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  7. Quality control of protein import into mammalian mitochondria.Protein science : a publication of the Protein Society · 2026
    Review
  8. In and out of the mitochondrial intermembrane space.Protein science : a publication of the Protein Society · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mitochondrial protein import stress.Nature cell biology · 2025
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Pharmacological Progress of Mitophagy Regulation.Current neuropharmacology · 2023
    Article

25 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

4 authors at 1 institution in 1 country.

Piotr BragoszewskiInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Agnieszka Gornicka
Malgorzata E Sztolsztener
Agnieszka Chacinska
International Institute of Molecular and Cell Biology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial precursor proteins are synthesized in the cytosol and subsequently imported into mitochondria. The import of mitochondrial intermembrane space proteins is coupled with their oxidative folding and governed by the mitochondrial intermembrane space import and assembly (MIA) pathway. The cytosolic steps that precede mitochondrial import are not well understood. We identified a role for the ubiquitin-proteasome system in the biogenesis of intermembrane space proteins. Interestingly, the function of the ubiquitin-proteasome system is not restricted to conditions of mitochondrial protein import failure. The ubiquitin-proteasome system persistently removes a fraction of intermembrane space proteins under physiological conditions, acting as a negative regulator in the biogenesis of this class of proteins. Thus, the ubiquitin-proteasome system plays an important role in determining the levels of proteins targeted to the intermembrane space of mitochondria.

Indexed as

Cation Transport ProteinsCopper Transport ProteinsCytosolIntracellular MembranesLeupeptinsMembrane ProteinsMembrane Transport ProteinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular ChaperonesMultienzyme ComplexesMutationProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitinbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCation Transport ProteinsCopper Transport ProteinsCOX17 protein, S cerevisiaeLeupeptinsMembrane ProteinsMembrane Transport ProteinsMIA40 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular ChaperonesMultienzyme ComplexesPet191 protein, S cerevisiaePRE1 protein, S cerevisiaePRE2 protein, S cerevisiaeProteasome Endopeptidase ComplexRPN13 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTIM10 protein, S cerevisiaeTIM13 protein, S cerevisiaeTim8 protein, S cerevisiaeTim9 protein, S cerevisiaeUbiquitinUbiquitinated Proteins

Identifiers

PMID23508107
PMCPMC3648063
OpenAlexW2168290116

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.