Evidence map›Paper›PMID 30277212›Full record

ArticleeLife2018

Cryo-EM structure of respiratory complex I at work.

Kristian Parey, Ulrich Brandt, Hao Xie, Deryck J Mills, Karin Siegmund, Janet Vonck, Werner Kühlbrandt, Volker Zickermann

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
6.1field-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

56 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Cyanobacterial Bioenergetics in Relation to Cellular Growth and Productivity.Advances in biochemical engineering/biotechnology · 2023
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Binding of Natural Inhibitors to Respiratory Complex I.Pharmaceuticals (Basel, Switzerland) · 2022
    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

8 authors at 2 institutions in 2 countries.

Kristian PareyDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID 0000-0002-4842-6479
Ulrich BrandtRadboud Institute for Molecular Life Sciences, Department of Pediatrics, Radboud University Medical Centre, Nijmegen, The Netherlands.
Hao XieDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Deryck J MillsDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Karin SiegmundMedical School, Institute of Biochemistry II, Goethe University Frankfurt, Frankfurt, Germany.
Janet VonckDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID 0000-0001-5659-8863
Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID 0000-0002-2013-4810
Volker ZickermannCluster of Excellence Macromolecular Complexes, Goethe University Frankfurt, Frankfurt, Germany.ORCID 0000-0001-8461-8817
Goethe University Frankfurt · DEMax Planck Institute of Biophysics · DE

Funding

Deutsche Forschungsgemeinschaft ZI 552/4-1Excellence Initiative of the German Federal and State Governments EXC 115Netherlands Organization for Scientific Research TOP grant 714.017.004
6 · The paper itself

Abstract

Mitochondrial complex I has a key role in cellular energy metabolism, generating a major portion of the proton motive force that drives aerobic ATP synthesis. The hydrophilic arm of the L-shaped ~1 MDa membrane protein complex transfers electrons from NADH to ubiquinone, providing the energy to drive proton pumping at distant sites in the membrane arm. The critical steps of energy conversion are associated with the redox chemistry of ubiquinone. We report the cryo-EM structure of complete mitochondrial complex I from the aerobic yeast

Indexed as

Amino Acid SequenceCryoelectron MicroscopyCrystallography, X-RayElectron Transport Complex IEnergy MetabolismFungal ProteinsMitochondriaModels, MolecularOxidation-ReductionOxygen ConsumptionProtein ConformationProton-Motive ForceSequence Homology, Amino AcidYarrowiaElectron Transport Complex IFungal Proteinsactive/deactive transitionmolecular biophysicsredox-linked proton translocationrespiratory complex Istructural biologyYarrowia lipolytica

Identifiers

PMID30277212
PMCPMC6168287
OpenAlexW2895328994

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.