Evidence map›Paper›PMID 33067417›Full record

ArticleNature communications2020

Structure of inhibitor-bound mammalian complex I.

Hannah R Bridges, Justin G Fedor, James N Blaza, Andrea Di Luca, Alexander Jussupow, Owen D Jarman, John J Wright, Ahmed-Noor A Agip, Ana P Gamiz-Hernandez, Maxie M Roessler and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
5.8field-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

64 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Hydration-Controlled Proton Transport in Respiratory Complex I.Journal of the American Chemical Society · 2026
    Article
  6. Emerging role of mitoNEET as mitochondrial sensor of hypoxia.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. A fixed mutation in the respiratory complex I impairs mitochondrial bioenergetics in the endangered Apennine brown bear.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

4 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

12 authors at 4 institutions in 3 countries.

Hannah R BridgesThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.ORCID 0000-0001-6890-6050
Justin G FedorThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.ORCID 0000-0003-3660-3818
James N BlazaThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.ORCID 0000-0001-5420-2116
Andrea Di LucaCenter for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany.ORCID 0000-0001-6138-2485
Alexander JussupowCenter for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany.ORCID 0000-0001-7851-2741
Owen D JarmanThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
John J WrightThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Ahmed-Noor A AgipThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Ana P Gamiz-HernandezCenter for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany.ORCID 0000-0002-0961-328X
Maxie M RoesslerDepartment of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus, London, W12 0BZ, UK.ORCID 0000-0002-5291-4328
Ville R I KailaCenter for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany. ville.kaila@dbb.su.se.ORCID 0000-0003-4464-6324
Judy HirstThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK. jh@mrc-mbu.cam.ac.uk.ORCID 0000-0001-8667-6797
University of Cambridge · GBStockholm University · SECenter for Integrated Protein Science Munich · DEImperial College London · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_U105663141Medical Research Council MC_UU_00015/2Medical Research Council MC_UU_00015/7Wellcome TrustWellcome Trust 108466/Z/15/Z
6 · The paper itself

Abstract

Respiratory complex I (NADH:ubiquinone oxidoreductase) captures the free energy from oxidising NADH and reducing ubiquinone to drive protons across the mitochondrial inner membrane and power oxidative phosphorylation. Recent cryo-EM analyses have produced near-complete models of the mammalian complex, but leave the molecular principles of its long-range energy coupling mechanism open to debate. Here, we describe the 3.0-Å resolution cryo-EM structure of complex I from mouse heart mitochondria with a substrate-like inhibitor, piericidin A, bound in the ubiquinone-binding active site. We combine our structural analyses with both functional and computational studies to demonstrate competitive inhibitor binding poses and provide evidence that two inhibitor molecules bind end-to-end in the long substrate binding channel. Our findings reveal information about the mechanisms of inhibition and substrate reduction that are central for understanding the principles of energy transduction in mammalian complex I.

Indexed as

AnimalsBinding SitesCryoelectron MicroscopyElectron Transport Complex IEnzyme InhibitorsFemaleMammalsMiceMice, Inbred C57BLMitochondria, HeartMolecular Dynamics SimulationOxidative PhosphorylationPyridinesElectron Transport Complex IEnzyme Inhibitorspiericidin APyridines

Identifiers

PMID33067417
PMCPMC7567858
OpenAlexW3092856399

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.