Evidence map›Paper›PMID 23676665›Full record

ArticleMolecular biology of the cell2013

Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells.

Manuel Fischer, Sebastian Horn, Anouar Belkacemi, Kerstin Kojer, Carmelina Petrungaro, Markus Habich, Muna Ali, Victoria Küttner, Melanie Bien, Frank Kauff and 3 more

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
5.2field-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

64 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Oxidation ofAntioxidants (Basel, Switzerland) · 2023
    Article
  13. Article
  14. Article
  15. Real-Time Monitoring of Hydrogen Peroxide Levels in Yeast and Mammalian Cells.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  16. Article
  17. Review
  18. Antioxidants (Basel, Switzerland) · 2022
    Review
  19. Review
  20. Review

4 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

13 authors at 3 institutions in 1 country.

Manuel FischerCellular Biochemistry, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Sebastian Horn
Anouar Belkacemi
Kerstin Kojer
Carmelina Petrungaro
Markus Habich
Muna Ali
Victoria Küttner
Melanie Bien
Frank Kauff
Jörn Dengjel
Johannes M Herrmann
Jan Riemer
University of Kaiserslautern · DEUniversity of Freiburg · DESaarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidation of cysteine residues to disulfides drives import of many proteins into the intermembrane space of mitochondria. Recent studies in yeast unraveled the basic principles of mitochondrial protein oxidation, but the kinetics under physiological conditions is unknown. We developed assays to follow protein oxidation in living mammalian cells, which reveal that import and oxidative folding of proteins are kinetically and functionally coupled and depend on the oxidoreductase Mia40, the sulfhydryl oxidase augmenter of liver regeneration (ALR), and the intracellular glutathione pool. Kinetics of substrate oxidation depends on the amount of Mia40 and requires tightly balanced amounts of ALR. Mia40-dependent import of Cox19 in human cells depends on the inner membrane potential. Our observations reveal considerable differences in the velocities of mitochondrial import pathways: whereas preproteins with bipartite targeting sequences are imported within seconds, substrates of Mia40 remain in the cytosol for several minutes and apparently escape premature degradation and oxidation.

Indexed as

AnimalsBiological AssayCytochrome ReductasesDisulfidesFibroblastsGene Expression RegulationGlutathioneHEK293 CellsHumansKineticsMembrane Potential, MitochondrialMiceMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsCHCHD4 protein, humanCOX19 protein, humanCytochrome ReductasesDisulfidesGFER protein, humanGlutathioneMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsOxidoreductases Acting on Sulfur Group DonorsSulfur Radioisotopes

Identifiers

PMID23676665
PMCPMC3708723
OpenAlexW2157485133

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.