Evidence map›Paper›PMID 22949654›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates.

Momi Iwata, Yang Lee, Tetsuo Yamashita, Takao Yagi, So Iwata, Alexander D Cameron, Megan J Maher

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 108 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
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  5. Article
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  7. Article
  8. Article
  9. Inhibitors of Type II NADH Dehydrogenase Enzyme: A Review.Current protein & peptide science · 2025
    Review
  10. Article
  11. The Warburg Effect is the result of faster ATP production by glycolysis than respiration.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Alternative oxidase blunts pseudohypoxia and photoreceptor degeneration due to RPE mitochondrial dysfunction.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Synthesis andACS infectious diseases · 2022
    Article
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  20. 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

7 authors at 5 institutions in 4 countries.

Momi IwataDivision of Molecular Biosciences, Imperial College, London, United Kingdom.
Yang Lee
Tetsuo Yamashita
Takao Yagi
So Iwata
Alexander D Cameron
Megan J Maher
Imperial College London · GBDiamond Light Source · GBKagawa University · JPKyoto University · JPScripps Research Institute · US

Funding

NADH-UBIQUINONE REDUCTASE OF PARACOCCUS DENITRIFICANSR01GM033712 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI YAGI, TAKAO · 1985 to 2011
$6.4M
Molecular Remedy of Mitochondrial DefectsR01EY020796 · NEI · SCRIPPS RESEARCH INSTITUTE, THE · PI YAGI, TAKAO · 2011 to 2015
$2.3M
Biotechnology and Biological Sciences Research Council BB/D019311/1Biotechnology and Biological Sciences Research Council BB/G023425/1NEI NIH HHS R01 EY020796NEI NIH HHS R01EY020796NIGMS NIH HHS R01 GM033712NIGMS NIH HHS R01GM033712Wellcome TrustWellcome Trust 062164/ Z/00/Z
6 · The paper itself

Abstract

Bioenergy is efficiently produced in the mitochondria by the respiratory system consisting of complexes I-V. In various organisms, complex I can be replaced by the alternative NADH-quinone oxidoreductase (NDH-2), which catalyzes the transfer of an electron from NADH via FAD to quinone, without proton pumping. The Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the matrix. A number of studies have investigated the potential use of Ndi1 as a therapeutic agent against complex I disorders, and the NDH-2 enzymes have emerged as potential therapeutic targets for treatments against the causative agents of malaria and tuberculosis. Here we present the crystal structures of Ndi1 in its substrate-free, NAD(+)- and ubiquinone- (UQ2) complexed states. The structures reveal that Ndi1 is a peripheral membrane protein forming an intimate dimer, in which packing of the monomeric units within the dimer creates an amphiphilic membrane-anchor domain structure. Crucially, the structures of the Ndi1-NAD(+) and Ndi1-UQ2 complexes show overlapping binding sites for the NAD(+) and quinone substrates.

Indexed as

Binding SitesCatalytic DomainCrystallography, X-RayCytoplasmDimerizationElectronsElectron Transport Complex IEscherichia coliLipidsMolecular ConformationMutationProtein Structure, TertiaryProtonsQuinonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsElectron Transport Complex ILipidsNdi1 protein, S cerevisiaeProtonsQuinonesSaccharomyces cerevisiae ProteinsWater

Identifiers

PMID22949654
PMCPMC3458368
OpenAlexW2062338036

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.