Evidence map›Paper›PMID 26182433›Full record

ArticleBioscience reports2015

A biophysical study on molecular physiology of the uncoupling proteins of the central nervous system.

Tuan Hoang, Miljan Kuljanin, Matthew D Smith, Masoud Jelokhani-Niaraki

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Frogs uncouple neural activity from oxygen consumption after hibernation.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
  6. Interconnected roles of mitochondrial carrier proteins ANT, PFrontiers in molecular biosciences · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. Uncoupling Proteins and Regulated Proton Leak in Mitochondria.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

4 authors at 2 institutions in 1 country.

Tuan HoangDepartment of Chemistry and Biochemistry, Wilfrid Laurier University, Waterloo, Ontario, Canada, N2L 3C5 Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada, N1G 2W1.
Miljan KuljaninDepartment of Chemistry and Biochemistry, Wilfrid Laurier University, Waterloo, Ontario, Canada, N2L 3C5.
Matthew D SmithDepartment of Biology, Wilfrid Laurier University, Waterloo, Ontario, Canada, N2L 3C5 Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada, N1G 2W1.
Masoud Jelokhani-NiarakiDepartment of Chemistry and Biochemistry, Wilfrid Laurier University, Waterloo, Ontario, Canada, N2L 3C5 Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada, N1G 2W1 mjelokhani@wlu.ca.
Wilfrid Laurier University · CAUniversity of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial inner membrane uncoupling proteins (UCPs) facilitate transmembrane (TM) proton flux and consequently reduce the membrane potential and ATP production. It has been proposed that the three neuronal human UCPs (UCP2, UCP4 and UCP5) in the central nervous system (CNS) play significant roles in reducing cellular oxidative stress. However, the structure and ion transport mechanism of these proteins remain relatively unexplored. Recently, we reported a novel expression system for obtaining functionally folded UCP1 in bacterial membranes and applied this system to obtain highly pure neuronal UCPs in high yields. In the present study, we report on the structure and function of the three neuronal UCP homologues. Reconstituted neuronal UCPs were dominantly helical in lipid membranes and transported protons in the presence of physiologically-relevant fatty acid (FA) activators. Under similar conditions, all neuronal UCPs also exhibited chloride transport activities that were partially inhibited by FAs. CD, fluorescence and MS measurements and semi-native gel electrophoresis collectively suggest that the reconstituted proteins self-associate in the lipid membranes. Based on SDS titration experiments and other evidence, a general molecular model for the monomeric, dimeric and tetrameric functional forms of UCPs in lipid membranes is proposed. In addition to their shared structural and ion transport features, neuronal UCPs differ in their conformations and proton transport activities (and possibly mechanism) in the presence of different FA activators. The differences in FA-activated UCP-mediated proton transport could serve as an essential factor in understanding and differentiating the physiological roles of UCP homologues in the CNS.

Indexed as

Models, MolecularProtein FoldingCentral Nervous SystemHumansIon ChannelsMitochondrial ProteinsNerve Tissue ProteinsProtein Structure, SecondaryIon ChannelsMitochondrial ProteinsNerve Tissue Proteinscentral nervous system (CNS)circular dichroism (CD) spectroscopyfatty acid (FA)membrane protein foldingmolecular associationproton transportreconstitutionuncoupling proteins (UCPs)

Identifiers

PMID26182433
PMCPMC4613710
OpenAlexW1788256667

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.