Evidence map›Paper›PMID 18323778›Full record

ArticleThe EMBO journal2008

Dimer ribbons of ATP synthase shape the inner mitochondrial membrane.

Mike Strauss, Götz Hofhaus, Rasmus R Schröder, Werner Kühlbrandt

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 333 papers.

0numbers the graph read from it
0cells of the map it votes in
333citing papers in PubMed
14.9field-weighted citation impact, top 1% 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

333 citing papers in PubMed, 660 citations in OpenAlex.

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  18. Subtomogram Averaging of Membrane Complexes in Organelle-Derived Vesicles.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
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  20. Article

273 more citing papers are in PubMed but not listed here.

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.

Mike StraussDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Götz Hofhaus
Rasmus R Schröder
Werner Kühlbrandt
Max Planck Institute of Biophysics · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP synthase converts the electrochemical potential at the inner mitochondrial membrane into chemical energy, producing the ATP that powers the cell. Using electron cryo-tomography we show that the ATP synthase of mammalian mitochondria is arranged in long approximately 1-microm rows of dimeric supercomplexes, located at the apex of cristae membranes. The dimer ribbons enforce a strong local curvature on the membrane with a 17-nm outer radius. Calculations of the electrostatic field strength indicate a significant increase in charge density, and thus in the local pH gradient of approximately 0.5 units in regions of high membrane curvature. We conclude that the mitochondrial cristae act as proton traps, and that the proton sink of the ATP synthase at the apex of the compartment favours effective ATP synthesis under proton-limited conditions. We propose that the mitochondrial ATP synthase organises itself into dimer ribbons to optimise its own performance.

Indexed as

AnimalsCattleComputer SimulationDimerizationElectric ConductivityHydrogen-Ion ConcentrationMitochondrial MembranesMitochondrial Proton-Translocating ATPasesModels, BiologicalProtein Structure, QuaternaryProtein Structure, SecondaryRatsStatic ElectricityTomographyMitochondrial Proton-Translocating ATPases

Identifiers

PMID18323778
PMCPMC2323265
OpenAlexW2090734611

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.