Evidence map›Paper›PMID 18761382›Full record

ReviewBiochimica et biophysica acta2009

Redox regulation of protein folding in the mitochondrial intermembrane space.

Carla M Koehler, Heather L Tienson

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. The role of thiols in antioxidant systems.Free radical biology & medicine · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015
    Review
  15. Review
  16. Folding and biogenesis of mitochondrial small Tim proteins.International journal of molecular sciences · 2013
    Review
  17. Article
  18. The power of yeast to model diseases of the powerhouse of the cell.Frontiers in bioscience (Landmark edition) · 2013
    Review
  19. Article
  20. Intermembrane space proteome of yeast mitochondria.Molecular & cellular proteomics : MCP · 2012
    Article
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

2 authors at 1 institution in 1 country.

Carla M KoehlerDepartment of Chemistry and Biochemistry, UCLA, Box 951569, Los Angeles, CA 90095-1569, USA. koehler@chem.ucla.edu
Heather L Tienson
University of California, Los Angeles · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Biogenesis of the mitochondrial inner membrane diversity supplementR01GM061721 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KOEHLER, CARLA M · 2000 to 2025
$8.1M
NIGMS NIH HHS 1R01GM61721NIGMS NIH HHS GM07185NIGMS NIH HHS R01 GM061721NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

Protein translocation pathways to the mitochondrial matrix and inner membrane have been well characterized. However, translocation into the intermembrane space, which was thought to be simply a modification of the traditional translocation pathways, is complex. The mechanism by which a subset of intermembrane space proteins, those with disulfide bonds, are translocated has been largely unknown until recently. Specifically, the intermembrane space proteins with disulfide bonds are imported via the mitochondrial intermembrane space assembly (MIA) pathway. Substrates are imported via a disulfide exchange relay with two components Mia40 and Erv1. This new breakthrough has resulted in novel concepts for assembly of proteins in the intermembrane space, suggesting that this compartment may be similar to that of the endoplasmic reticulum and the prokaryotic periplasm. As a better understanding of this pathway emerges, new paradigms for thiol-disulfide exchange mechanisms may be developed. Given that the intermembrane space is important for disease processes including apoptosis and neurodegeneration, new roles in regulation by oxidation-reduction chemistry seem likely to be relevant.

Indexed as

AnimalsHumansMitochondrial MembranesMitochondrial ProteinsModels, BiologicalOxidation-ReductionProtein FoldingProtein TransportMitochondrial Proteins

Identifiers

PMID18761382
PMCPMC4099470
OpenAlexW2098842133

What OpenQuestion holds

Textmetadata
LicenceTDM
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.