Evidence map›Paper›PMID 25472962›Full record

ArticleAmerican journal of physiology. Cell physiology2015

Effect of p53 on mitochondrial morphology, import, and assembly in skeletal muscle.

Ayesha Saleem, Sobia Iqbal, Yuan Zhang, David A Hood

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Mutant p53 binds RNA to drive mitochondrial dysfunction.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. IsKidney medicine · 2025
    Article
  6. Article
  7. Mitochondrial Biogenesis in Skeletal Muscle.Advances in experimental medicine and biology · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Exercise is mitochondrial medicine for muscle.Sports medicine and health science · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

4 authors at 1 institution in 1 country.

Ayesha SaleemSchool of Kinesiology and Health Science, York University, Toronto, Ontario, Canada; and Muscle Health Research Centre, York University, Toronto, Ontario, Canada.
Sobia IqbalSchool of Kinesiology and Health Science, York University, Toronto, Ontario, Canada; and Muscle Health Research Centre, York University, Toronto, Ontario, Canada.
Yuan ZhangSchool of Kinesiology and Health Science, York University, Toronto, Ontario, Canada; and Muscle Health Research Centre, York University, Toronto, Ontario, Canada.
David A HoodSchool of Kinesiology and Health Science, York University, Toronto, Ontario, Canada; and Muscle Health Research Centre, York University, Toronto, Ontario, Canada dhood@yorku.ca.
York University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The purpose of this study was to investigate whether p53 regulates mitochondrial function via changes in mitochondrial protein import, complex IV (COX) assembly, or the expression of key proteins involved in mitochondrial dynamics and degradation. Mitochondria from p53 KO mice displayed ultra-structural alterations and were more punctate in appearance. This was accompanied by protein-specific alterations in fission, fusion, and mitophagy-related proteins. However, matrix-destined protein import into subsarcolemmal or intermyofibrillar mitochondria was unaffected in the absence of p53, despite mitochondrial subfraction-specific reductions in Tom20, Tim23, mtHsp70, and mtHsp60 in the knockout (KO) mitochondria. Complex IV activity in isolated mitochondria was also unchanged in KO mice, but two-dimensional blue native-PAGE revealed a reduction in the assembly of complex IV within the IMF fractions from KO mice in tandem with lower levels of the assembly protein Surf1. This observed defect in complex IV assembly may facilitate the previously documented impairment in mitochondrial function in p53 KO mice. We suspect that these morphological and functional impairments in mitochondria drive a decreased reliance on mitochondrial respiration as a means of energy production in skeletal muscle in the absence of p53.

Indexed as

Mitochondrial DynamicsAnimalsAutophagyCell RespirationChaperonin 60Electron Transport Complex IVEnergy MetabolismHSP70 Heat-Shock ProteinsMembrane ProteinsMembrane Transport ProteinsMice, KnockoutMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMitochondria, MuscleMitophagyChaperonin 60Electron Transport Complex IVHSP70 Heat-Shock ProteinsHspd1 protein, mouseMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsReceptors, Cell SurfaceSurf-1 proteinTimm23 protein, mouseTomm20 protein, mouseTumor Suppressor Protein p53cytochrome c oxidase assemblyfission/fusionmitophagyprotein import machinery

Identifiers

PMID25472962
PMCPMC4329426
OpenAlexW2123065811

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.