Evidence map›Paper›PMID 28186490›Full record

ArticleeLife2017

Atomistic simulations indicate the c-subunit ring of the F

Wenchang Zhou, Fabrizio Marinelli, Corrine Nief, José D Faraldo-Gómez

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
6.5field-weighted citation impact, top 2% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Review
  6. Mitochondrial Permeability Transition in Stem Cells, Development, and Disease.Advances in experimental medicine and biology · 2023
    Review
  7. Article
  8. Review
  9. ATP synthase FCellular and molecular life sciences : CMLS · 2022
    Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Diabetes Mellitus, Mitochondrial Dysfunction and CaInternational journal of molecular sciences · 2020
    Review
  15. Article
  16. Dysfunction of Mitochondrial CaFrontiers in cell and developmental biology · 2020
    Review
  17. Review
  18. Review
  19. Article
  20. Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

4 authors at 1 institution in 1 country.

Wenchang ZhouTheoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, United States.ORCID 0000-0003-0397-1032
Fabrizio MarinelliTheoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, United States.
Corrine NiefTheoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, United States.
José D Faraldo-GómezTheoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, United States.ORCID 0000-0001-7224-7676
National Institutes of Health · US

Funding

Molecular Mechanisms in Membrane Bioenergetics, Transport and SignalingZIAHL006203 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FARALDO-GÓMEZ, JOSE · 2015 to 2023
$15.4M
6 · The paper itself

Abstract

Pathological metabolic conditions such as ischemia induce the rupture of the mitochondrial envelope and the release of pro-apoptotic proteins, leading to cell death. At the onset of this process, the inner mitochondrial membrane becomes depolarized and permeable to osmolytes, proposedly due to the opening of a non-selective protein channel of unknown molecular identity. A recent study purports that this channel, referred to as Mitochondrial Permeability Transition Pore (MPTP), is formed within the c-subunit ring of the ATP synthase, upon its dissociation from the catalytic domain of the enzyme. Here, we examine this claim for two c-rings of different lumen width, through calculations of their ion conductance and selectivity based on all-atom molecular dynamics simulations. We also quantify the likelihood that the lumen of these c-rings is in a hydrated, potentially conducting state rather than empty or blocked by lipid molecules. These calculations demonstrate that the structure and biophysical properties of a correctly assembled c-ring are inconsistent with those attributed to the MPTP.

Indexed as

Mitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesMolecular Dynamics SimulationSaccharomyces cerevisiaeF1F0-ATP synthaseMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesapoptosisbioenergeticsbiophysicsion channelsmitochondriamolecular dynamicsnonestructural biology

Identifiers

PMID28186490
PMCPMC5323039
OpenAlexW2586483729

What OpenQuestion holds

Textmetadata
LicenceCC0
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.