Evidence map›Paper›PMID 40738953›Full record

ArticleCommunications chemistry2025

Cardiolipin acyl chain composition tailors the conformation of mammalian ATP synthase dimers.

M Makowski, V G Almendro-Vedia, I López-Montero

Abstract read
In one paragraph

Article in Communications chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. A planar dimer of bovine ATP synthase.Cell death and differentiation · 2026
    Article
  2. Article
  3. Review
  4. 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.

M MakowskiDepartamento de Química Física, Facultad de Ciencias Químicas de la Universidad Complutense de Madrid, Madrid, Spain. marmakow@ucm.es.ORCID http://orcid.org/0000-0001-6929-6143
V G Almendro-VediaInstituto Pluridisciplinar, Universidad Complutense de Madrid, Universidad Complutense de Madrid, Madrid, Spain.
I López-MonteroDepartamento de Química Física, Facultad de Ciencias Químicas de la Universidad Complutense de Madrid, Madrid, Spain. ivanlopez@quim.ucm.es.ORCID http://orcid.org/0000-0001-8131-6063

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interplay between ATP synthase dimers and the four-tailed lipid cardiolipin (CL) shapes mitochondrial cristae structure and function. In the mitochondrial disorder Barth syndrome (BTHS), cristae membranes accumulate a less unsaturated, three-tailed form of cardiolipin (MLCL). These cristae become structurally and functionally compromised through mechanisms poorly understood. We have studied through molecular dynamics simulations how BTHS lipid composition affects the conformation of the ATP synthase dimer. The wedge-shaped transmembrane region of the ATP synthase dimer attracts cardiolipins through shape complementarity. MLCL showed decreased affinity for the dimer interface than CLs of the healthy model. A more heterogeneous lipid environment with a higher elastic strain promoted a dimer conformation that would stabilize wider intracrista spaces, and hence, less efficient OXPHOS reactions in BTHS. Our results provide clues on the role played by the CL acyl chain composition in the architecture and function of mitochondria in health and BTHS.

Identifiers

PMID40738953
PMCPMC12311173

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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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 Socratic graph.