Evidence map›Paper›PMID 31543713›Full record

ReviewThe Yale journal of biology and medicine2019

Phosphorylation of OXPHOS Machinery Subunits: Functional Implications in Cell Biology and Disease.

Ernesto Castellanos, Nathan James Lanning

Abstract readReview
In one paragraph

Review in The Yale journal of biology and medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Serine phosphorylation facilitates protein degradation by the human mitochondrial ClpXP protease.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Mitochondrial sAC-cAMP-PKA Axis Modulates the ΔΨInternational journal of molecular sciences · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Mitochondrial and Neuronal Dysfunctions in L1 Mutant Mice.International journal of molecular sciences · 2022
    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

2 authors at 1 institution in 1 country.

Ernesto CastellanosDepartment of Biochemistry, California State University, Los Angeles, CA.
Nathan James LanningDepartment of Biological Sciences, California State University, Los Angeles, CA.
California State University Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The complexes of the electron transport chain and ATP synthase comprise the oxidative phosphorylation (OXPHOS) system. The reactions of OXPHOS generate the mitochondrial membrane potential, drive the majority of ATP production in respiring cells, and contribute significantly to cellular reactive oxygen species (ROS). Regulation of OXPHOS is therefore critical to maintain cellular homeostasis. OXPHOS machinery subunits have been found to be highly phosphorylated, implicating this post-translational modification as a means whereby OXPHOS is regulated. Multiple lines of evidence now reveal the diverse mechanisms by which phosphorylation of OXPHOS machinery serve to regulate individual complex stability and activity as well as broader cellular functions. From these mechanistic studies of OXPHOS machinery phosphorylation, it is now clear that many aspects of human health and disease are potentially impacted by phosphorylation of OXPHOS complexes. This mini-review summarizes recent studies that provide robust mechanistic detail related to OXPHOS subunit phosphorylation.

Indexed as

Cell BiologyOxidative PhosphorylationAnimalsElectron Transport Chain Complex ProteinsHumansMitochondriaMitochondrial DiseasesProtein SubunitsElectron Transport Chain Complex ProteinsProtein Subunitselectron transport chainmitochondriaoxphosphosphorylation

Identifiers

PMID31543713
PMCPMC6747953
OpenAlexW2988440179

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.