Evidence map›Paper›PMID 29915388›Full record

ArticleNature structural & molecular biology2018

Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states.

Ahmed-Noor A Agip, James N Blaza, Hannah R Bridges, Carlo Viscomi, Shaun Rawson, Stephen P Muench, Judy Hirst

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
10.9field-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

150 citing papers in PubMed, 239 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Hydration-Controlled Proton Transport in Respiratory Complex I.Journal of the American Chemical Society · 2026
    Article
  5. Article
  6. Article
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  8. Article
  9. Global conformations ofScience advances · 2025
    Article
  10. Article
  11. Respiratory complex IIIbioRxiv : the preprint server for biology · 2025
    Article
  12. Article
  13. Dietary effects on the retina of hamsters.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  14. Article
  15. Formation of ICell metabolism · 2025
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

90 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

7 authors at 2 institutions in 1 country.

Ahmed-Noor A AgipThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
James N BlazaThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.ORCID 0000-0001-5420-2116
Hannah R BridgesThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Carlo ViscomiThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Shaun RawsonSchool of Biomedical Sciences, Faculty of Biological Sciences and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.
Stephen P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.ORCID 0000-0001-6869-4414
Judy HirstThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK. jh@mrc-mbu.cam.ac.uk.ORCID 0000-0001-8667-6797
University of Cambridge · GBUniversity of Leeds · GB

Funding

Medical Research Council MC_U105663141Medical Research Council MC_UP_1002/1Medical Research Council MC_UU_00015/2Medical Research Council MC_UU_00015/8Wellcome Trust
6 · The paper itself

Abstract

Complex I (NADH:ubiquinone oxidoreductase) uses the reducing potential of NADH to drive protons across the energy-transducing inner membrane and power oxidative phosphorylation in mammalian mitochondria. Recent cryo-EM analyses have produced near-complete models of all 45 subunits in the bovine, ovine and porcine complexes and have identified two states relevant to complex I in ischemia-reperfusion injury. Here, we describe the 3.3-Å structure of complex I from mouse heart mitochondria, a biomedically relevant model system, in the 'active' state. We reveal a nucleotide bound in subunit NDUFA10, a nucleoside kinase homolog, and define mechanistically critical elements in the mammalian enzyme. By comparisons with a 3.9-Å structure of the 'deactive' state and with known bacterial structures, we identify differences in helical geometry in the membrane domain that occur upon activation or that alter the positions of catalytically important charged residues. Our results demonstrate the capability of cryo-EM analyses to challenge and develop mechanistic models for mammalian complex I.

Indexed as

AnimalsBinding SitesCryoelectron MicroscopyElectron Transport Complex IEnzyme ActivationMiceMitochondria, HeartModels, MolecularNADH DehydrogenaseNucleotidesPhospholipidsProtein Structural ElementsProtein Structure, QuaternaryProtein SubunitsUbiquinoneElectron Transport Complex INADH DehydrogenaseNdufA10 protein, mouseNucleotidesPhospholipidsProtein SubunitsUbiquinone

Identifiers

PMID29915388
PMCPMC6054875
OpenAlexW2806917274

What OpenQuestion holds

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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.