Evidence map›Paper›PMID 21545356›Full record

ArticleThe Biochemical journal2011

A scaffold of accessory subunits links the peripheral arm and the distal proton-pumping module of mitochondrial complex I.

Heike Angerer, Klaus Zwicker, Zibiernisha Wumaier, Lucie Sokolova, Heinrich Heide, Mirco Steger, Silke Kaiser, Esther Nübel, Bernhard Brutschy, Michael Radermacher and 2 more

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.2field-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

32 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cytonuclear integration and co-evolution.Nature reviews. Genetics · 2018
    Review
  11. Article
  12. Article
  13. Structure of subcomplex Iβ of mammalian respiratory complex I leads to new supernumerary subunit assignments.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Accessory NUMM (NDUFS6) subunit harbors a Zn-binding site and is essential for biogenesis of mitochondrial complex I.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 1 institution in 1 country.

Heike AngererMedical School, Center for Membrane Proteomics, Goethe-University, Frankfurt am Main, Germany.
Klaus Zwicker
Zibiernisha Wumaier
Lucie Sokolova
Heinrich Heide
Mirco Steger
Silke Kaiser
Esther Nübel
Bernhard Brutschy
Michael Radermacher
Ulrich Brandt
Volker Zickermann
Goethe University Frankfurt · DE

Funding

3D Structure of Membrane ProteinsR01GM068650 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI RADERMACHER, MICHAEL · 2003 to 2013
$2.4M
NIGMS NIH HHS 2R01 GM068650NIGMS NIH HHS R01 GM068650
6 · The paper itself

Abstract

Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is a very large membrane protein complex with a central function in energy metabolism. Complex I from the aerobic yeast Yarrowia lipolytica comprises 14 central subunits that harbour the bioenergetic core functions and at least 28 accessory subunits. Despite progress in structure determination, the position of individual accessory subunits in the enzyme complex remains largely unknown. Proteomic analysis of subcomplex Iδ revealed that it lacked eleven subunits, including the central subunits ND1 and ND3 forming the interface between the peripheral and the membrane arm in bacterial complex I. This unexpected observation provided insight into the structural organization of the connection between the two major parts of mitochondrial complex I. Combining recent structural information, biochemical evidence on the assignment of individual subunits to the subdomains of complex I and sequence-based predictions for the targeting of subunits to different mitochondrial compartments, we derived a model for the arrangement of the subunits in the membrane arm of mitochondrial complex I.

Indexed as

Electron Transport Complex IMitochondriaModels, MolecularProtein SubunitsProton PumpsYarrowiaElectron Transport Complex IProtein SubunitsProton Pumps

Identifiers

PMID21545356
PMCPMC3273332
OpenAlexW2150935703

What OpenQuestion holds

Textmetadata
LicenceTDM
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.