Evidence map›Paper›PMID 18522805›Full record

ReviewBiochimica et biophysica acta2009

Suppression mechanisms of COX assembly defects in yeast and human: insights into the COX assembly process.

Antoni Barrientos, Karine Gouget, Darryl Horn, Ileana C Soto, Flavia Fontanesi

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 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed, 100 citations in OpenAlex.

  1. Yeast as a Model for Human Disease.International journal of molecular sciences · 2026
    Review
  2. Review
  3. The [PSIMolecular biology of the cell · 2022
    Article
  4. Comprehensive Characterization of MutantJournal of microbiology and biotechnology · 2022
    Article
  5. PTENα is responsible for protection of brain against oxidative stress during aging.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Cox15 interacts with the cytochromeThe Journal of biological chemistry · 2018
    Article
  12. Review
  13. The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.Biochimica et biophysica acta. Molecular cell research · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Antoni BarrientosDepartment of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA. abarrientos@med.miami.edu
Karine Gouget
Darryl Horn
Ileana C Soto
Flavia Fontanesi
University of Miami · US

Funding

CYTOCHROME C OXIDASE IN HEALTH AND DISEASER01GM071775 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2006 to 2015
$3.1M
NIGMS NIH HHS GM071775ANIGMS NIH HHS R01 GM071775Telethon GFP05008
6 · The paper itself

Abstract

Eukaryotic cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. COX is a multimeric enzyme formed by subunits of dual genetic origin whose assembly is intricate and highly regulated. In addition to the structural subunits, a large number of accessory factors are required to build the holoenzyme. The function of these factors is required in all stages of the assembly process. They are relevant to human health because devastating human disorders have been associated with mutations in nuclear genes encoding conserved COX assembly factors. The study of yeast strains and human cell lines from patients carrying mutations in structural subunits and COX assembly factors has been invaluable to attain the current state of knowledge, even if still fragmentary, of the COX assembly process. After the identification of the genes involved, the isolation and characterization of genetic and metabolic suppressors of COX assembly defects, reviewed here, have become a profitable strategy to gain insight into their functions and the pathways in which they operate. Additionally, they have the potential to provide useful information for devising therapeutic approaches to combat human disorders associated with COX deficiency.

Indexed as

AnimalsCytochrome-c Oxidase DeficiencyElectron Transport Complex IVHemeHumansMammalsModels, BiologicalSaccharomyces cerevisiaeElectron Transport Complex IVHemeheme a

Identifiers

PMID18522805
PMCPMC2644423
OpenAlexW2123634642

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.