Evidence map›Paper›PMID 35163451›Full record

ReviewInternational journal of molecular sciences2022

Uncoupling Proteins and Regulated Proton Leak in Mitochondria.

Afshan Ardalan, Matthew D Smith, Masoud Jelokhani-Niaraki

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Interconnected roles of mitochondrial carrier proteins ANT, PFrontiers in molecular biosciences · 2025
    Article
  8. Article
  9. Article
  10. International journal of molecular sciences · 2023
    Article
  11. Article
  12. Review
  13. Article
  14. Membrane Proteins: Structure, Function and Motion.International journal of molecular sciences · 2022
    Article
  15. Review
  16. Uncoupling Proteins as Therapeutic Targets for Neurodegenerative Diseases.International journal of molecular sciences · 2022
    Review
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

3 authors at 1 institution in 1 country.

Afshan ArdalanDepartment of Chemistry and Biochemistry, Wilfrid Laurier University, Waterloo, ON N2L 3C5, Canada.
Matthew D SmithDepartment of Biology, Wilfrid Laurier University, Waterloo, ON N2L 3C5, Canada.ORCID 0000-0002-2855-5126
Masoud Jelokhani-NiarakiDepartment of Chemistry and Biochemistry, Wilfrid Laurier University, Waterloo, ON N2L 3C5, Canada.ORCID 0000-0003-0599-0448
Wilfrid Laurier University · CA

Funding

Canada Foundation for Innovation 6786Natural Sciences and Engineering Research Council 05900
6 · The paper itself

Abstract

Higher concentration of protons in the mitochondrial intermembrane space compared to the matrix results in an electrochemical potential causing the back flux of protons to the matrix. This proton transport can take place through ATP synthase complex (leading to formation of ATP) or can occur via proton transporters of the mitochondrial carrier superfamily and/or membrane lipids. Some mitochondrial proton transporters, such as uncoupling proteins (UCPs), transport protons as their general regulating function; while others are symporters or antiporters, which use the proton gradient as a driving force to co-transport other substrates across the mitochondrial inner membrane (such as phosphate carrier, a symporter; or aspartate/glutamate transporter, an antiporter). Passage (or leakage) of protons across the inner membrane to matrix from any route other than ATP synthase negatively impacts ATP synthesis. The focus of this review is on regulated proton transport by UCPs. Recent findings on the structure and function of UCPs, and the related research methodologies, are also critically reviewed. Due to structural similarity of members of the mitochondrial carrier superfamily, several of the known structural features are potentially expandable to all members. Overall, this report provides a brief, yet comprehensive, overview of the current knowledge in the field.

Indexed as

AnimalsGene Expression RegulationHumansIon TransportMembrane Potential, MitochondrialMitochondriaMitochondrial Uncoupling ProteinsModels, MolecularProtein ConformationMitochondrial Uncoupling ProteinsADP/ATP carrieralternating access mechanismATP synthesisbiphasic proton transport modelmembrane protein oligomerizationmembrane protein structure and functionmitochondrial carriersreactive oxygen species controlregulation and mechanism of proton transportuncoupling proteins

Identifiers

PMID35163451
PMCPMC8835771
OpenAlexW4213200254

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.