Evidence map›Paper›PMID 28096380›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.

Alexander W Mühleip, Caroline E Dewar, Achim Schnaufer, Werner Kühlbrandt, Karen M Davies

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Proteolytic processing of the unique FScientific reports · 2026
    Article
  6. Article
  7. Review
  8. Why Euglenozoans.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. ATP synthase FCellular and molecular life sciences : CMLS · 2022
    Review
  17. Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022
    Article
  18. Review
  19. Article
  20. Article
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

5 authors at 3 institutions in 2 countries.

Alexander W MühleipDepartment of Structural Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.
Caroline E DewarInstitute of Immunology and Infection Research and Centre for Immunity, Infection, and Evolution, University of Edinburgh, Edinburgh EH9 3FL, United Kingdom.
Achim SchnauferInstitute of Immunology and Infection Research and Centre for Immunity, Infection, and Evolution, University of Edinburgh, Edinburgh EH9 3FL, United Kingdom.
Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany werner.kuehlbrandt@biophys.mpg.de KMDavies@lbl.gov.
Karen M DaviesDepartment of Structural Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany werner.kuehlbrandt@biophys.mpg.de KMDavies@lbl.gov.
Max Planck Institute of Biophysics · DECentre for Immunity, Infection and Evolution · GBUniversity of Edinburgh · GB

Funding

Medical Research Council G0600129Medical Research Council MR/L019701/1
6 · The paper itself

Abstract

We used electron cryotomography and subtomogram averaging to determine the in situ structures of mitochondrial ATP synthase dimers from two organisms belonging to the phylum euglenozoa: Trypanosoma brucei, a lethal human parasite, and Euglena gracilis, a photosynthetic protist. At a resolution of 32.5 Å and 27.5 Å, respectively, the two structures clearly exhibit a noncanonical F

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsCatalysisCatalytic DomainConsensus SequenceDimerizationEuglena gracilisMitochondriaModels, MolecularProtein ConformationProton-Translocating ATPasesProtozoan ProteinsRotationSequence AlignmentSequence Homology, Amino AcidAdenosine TriphosphateProton-Translocating ATPasesProtozoan Proteinselectron cryotomographymitochondrial ATP synthaserotary catalysissubtomogram averagingtrypanosome

Identifiers

PMID28096380
PMCPMC5293049
OpenAlexW2577415744

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.