Evidence map›Paper›PMID 27786441›Full record

ArticleBiochemistry2016

Lipid-Loving ANTs: Molecular Simulations of Cardiolipin Interactions and the Organization of the Adenine Nucleotide Translocase in Model Mitochondrial Membranes.

George Hedger, Sarah L Rouse, Jan Domański, Matthieu Chavent, Heidi Koldsø, Mark S P Sansom

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Sketching microprotein portraits.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Protein methylation in mitochondria.The Journal of biological chemistry · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

George HedgerDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
Sarah L RouseDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
Jan DomańskiDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
Matthieu ChaventDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
Heidi KoldsøDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
Mark S P SansomDepartment of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
D. E. Shaw Research · US

Funding

Biotechnology and Biological Sciences Research Council BB/I019855/1
6 · The paper itself

Abstract

The exchange of ADP and ATP across the inner mitochondrial membrane is a fundamental cellular process. This exchange is facilitated by the adenine nucleotide translocase, the structure and function of which are critically dependent on the signature phospholipid of mitochondria, cardiolipin (CL). Here we employ multiscale molecular dynamics simulations to investigate CL interactions within a membrane environment. Using simulations at both coarse-grained and atomistic resolutions, we identify three CL binding sites on the translocase, in agreement with those seen in crystal structures and inferred from nuclear magnetic resonance measurements. Characterization of the free energy landscape for lateral lipid interaction via potential of mean force calculations demonstrates the strength of interaction compared to those of binding sites on other mitochondrial membrane proteins, as well as their selectivity for CL over other phospholipids. Extending the analysis to other members of the family, yeast Aac2p and mouse uncoupling protein 2, suggests a degree of conservation. Simulation of large patches of a model mitochondrial membrane containing multiple copies of the translocase shows that CL interactions persist in the presence of protein-protein interactions and suggests CL may mediate interactions between translocases. This study provides a key example of how computational microscopy may be used to shed light on regulatory lipid-protein interactions.

Indexed as

Molecular Dynamics SimulationAdenine Nucleotide Translocator 1AnimalsBinding SitesCardiolipinsCattleCrystallography, X-RayMagnetic Resonance SpectroscopyMiceMitochondrial ADP, ATP TranslocasesMitochondrial MembranesProtein BindingProtein DomainsSaccharomyces cerevisiae ProteinsThermodynamicsUncoupling Protein 2Adenine Nucleotide Translocator 1CardiolipinsMitochondrial ADP, ATP TranslocasesPET9 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUncoupling Protein 2

Identifiers

PMID27786441
PMCPMC5120876
OpenAlexW2540686316

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.