Evidence map›Paper›PMID 22219186›Full record

ArticleThe Journal of biological chemistry2012

Selective Oma1 protease-mediated proteolysis of Cox1 subunit of cytochrome oxidase in assembly mutants.

Oleh Khalimonchuk, Mi-Young Jeong, Talina Watts, Elliott Ferris, Dennis R Winge

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

42 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. OMA1-An integral membrane protease?Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  8. Quality control of the mitochondrial proteome.Nature reviews. Molecular cell biology · 2021
    Review
  9. Review
  10. Article
  11. The Role of Reactive Oxygen Species in the Life Cycle of the Mitochondrion.International journal of molecular sciences · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Mitochondrial Proteolysis and Metabolic Control.Cold Spring Harbor perspectives in biology · 2019
    Review
  16. Article
  17. Article
  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.

Oleh KhalimonchukDepartment of Medicine and Biochemistry, University of Utah Health Sciences Center, Salt Lake City, Utah 84132, USA.
Mi-Young Jeong
Talina Watts
Elliott Ferris
Dennis R Winge
University of Utah · US

Funding

METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR37ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1999 to 2008
$4.1M
METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR01ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1985 to 2013
$2.3M
NIEHS NIH HHS ES03817NIEHS NIH HHS R01 ES003817NIEHS NIH HHS R37 ES003817
6 · The paper itself

Abstract

Stalled biogenesis of the mitochondrial cytochrome c oxidase (CcO) complex results in degradation of subunits containing redox cofactors. The conserved Oma1 metalloproteinase mediates facile Cox1 degradation in cells lacking the Coa2 assembly factor, but not in a series of other mutants stalled in CcO maturation. Oma1 is activated in coa2Δ cells, but the selective Cox1 degradation does not arise merely from its activation. Oma1 is also active in cells with dysfunctional mitochondria and cox11Δ cells impaired in CcO maturation, but this activation does not result in Oma1-mediated Cox1 degradation. The facile and selective degradation of Cox1 in coa2Δ cells, relative to other CcO assembly mutants, is likely due to impaired hemylation and subsequent misfolding of the subunit. Specific Cox1 proteolysis in coa2Δ cells arises from a combination of Oma1 activation and a susceptible conformation of Cox1.

Indexed as

ProteolysisElectron Transport Complex IVEnzyme ActivationMembrane ProteinsMetalloproteasesMitochondriaMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCoa2 protein, S cerevisiaeCox1 protein, S cerevisiaeElectron Transport Complex IVMembrane ProteinsMetalloproteasesOma1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22219186
PMCPMC3293553
OpenAlexW2023922838

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.