Evidence map›Paper›PMID 29093463›Full record

ArticleNature communications2017

INA complex liaises the F

Nataliia Naumenko, Marcel Morgenstern, Robert Rucktäschel, Bettina Warscheid, Peter Rehling

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Atp23p and Atp10p coordinate to regulate the assembly of yeast mitochondrial ATP synthase.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  9. Assembly of the peripheral stalk of ATP synthase in human mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Review
  15. Article
  16. Article
  17. Assembling the mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Assembly of the membrane domain of ATP synthase in human mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018
    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

5 authors at 3 institutions in 1 country.

Nataliia NaumenkoDepartment of Cellular Biochemistry, University Medical Center Göttingen, GZMB, D-37073, Göttingen, Germany.
Marcel MorgensternDepartment of Biochemistry and Functional Proteomics, Faculty of Biology, University Freiburg, D-79104, Freiburg, Germany.
Robert RucktäschelDepartment of Cellular Biochemistry, University Medical Center Göttingen, GZMB, D-37073, Göttingen, Germany.
Bettina WarscheidDepartment of Biochemistry and Functional Proteomics, Faculty of Biology, University Freiburg, D-79104, Freiburg, Germany.
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Göttingen, GZMB, D-37073, Göttingen, Germany. Peter.Rehling@medizin.uni-goettingen.de.
University of Freiburg · DEUniversity of Göttingen · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The F

Indexed as

ProtonsAdenosine DiphosphateAdenosine TriphosphateGene Expression Regulation, FungalMitochondrial MembranesMitochondrial Proton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine DiphosphateAdenosine TriphosphateATP6 protein, S cerevisiaeF1F0-ATP synthaseINA17 protein, S cerevisiaeINA22 protein, S cerevisiaeMitochondrial Proton-Translocating ATPasesOLI1 protein, S cerevisiaeProtonsSaccharomyces cerevisiae Proteins

Identifiers

PMID29093463
PMCPMC5665977
OpenAlexW2766011986

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.