Evidence map›Paper›PMID 23142977›Full record

ArticleNature structural & molecular biology2012

Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution.

Samir Benlekbir, Stephanie A Bueler, John L Rubinstein

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.6field-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

55 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
    Article
  3. Article
  4. Structural basis of V-ATPase VProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. Article
  7. The V-ATPases in cancer and cell death.Cancer gene therapy · 2022
    Review
  8. Coordinated conformational changes in the VNature structural & molecular biology · 2022
    Article
  9. Article
  10. Toosendanin, a novel potent vacuolar-type HInternational journal of biological sciences · 2022
    Article
  11. Review
  12. Structure of Ycf1p reveals the transmembrane domain TMD0 and the regulatory region of ABCC transporters.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Structural comparison of the vacuolar and Golgi V-ATPases fromProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Review
  17. Article
  18. The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018
    Review
  19. Atomic model for the dimeric FScience (New York, N.Y.) · 2017
    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

3 authors at 2 institutions in 1 country.

Samir BenlekbirMolecular Structure and Function Program, The Hospital for Sick Children Research Institute, Toronto, Ontario, Canada.
Stephanie A Bueler
John L Rubinstein
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research MOP 81294
6 · The paper itself

Abstract

Vacuolar-type ATPases (V-type ATPases) in eukaryotic cells are large membrane protein complexes that acidify various intracellular compartments. The enzymes are regulated by dissociation of the V(1) and V(O) regions of the complex. Here we present the structure of the Saccharomyces cerevisiae V-type ATPase at 11-Å resolution by cryo-EM of protein particles in ice. The structure explains many cross-linking and protein interaction studies. Docking of crystal structures suggests that inhibition of ATPase activity by the dissociated V(1) region involves rearrangement of the N- and C-terminal domains of subunit H and also suggests how this inhibition is triggered upon dissociation. We provide support for this model by demonstrating that mutation of subunit H to increase the rigidity of the linker between its two domains decreases its ability to inhibit ATPase activity.

Indexed as

Cryoelectron MicroscopyProtein ConformationSaccharomyces cerevisiaeVacuolar Proton-Translocating ATPasesVacuolar Proton-Translocating ATPases

Identifiers

PMID23142977
OpenAlexW2033106369

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.