Evidence map›Paper›PMID 19387495›Full record

ArticleThe EMBO journal2009

Inter-subunit interaction of gastric H+,K+-ATPase prevents reverse reaction of the transport cycle.

Kazuhiro Abe, Kazutoshi Tani, Tomohiro Nishizawa, Yoshinori Fujiyoshi

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. 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
4.7field-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

32 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Review
  3. A single KeLife · 2019
    Article
  4. Article
  5. KScientific reports · 2018
    Article
  6. Article
  7. The cryo-EM structure of gastric HScientific reports · 2017
    Article
  8. Article
  9. Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. Development of the field of structural physiology.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2015
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Pharmacokinetics and pharmacodynamics of the proton pump inhibitors.Journal of neurogastroenterology and motility · 2013
    Article
  18. Review
  19. Active detergent-solubilized H+,K+-ATPase is a monomer.The Journal of biological chemistry · 2012
    Article
  20. Cryo-EM structure of gastric H+,K+-ATPase with a single occupied cation-binding site.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Kazuhiro AbeDepartment of Biophysics, Faculty of Science, Kyoto University, Kyoto, Japan.
Kazutoshi Tani
Tomohiro Nishizawa
Yoshinori Fujiyoshi
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gastric H(+),K(+)-ATPase is an ATP-driven proton pump responsible for generating a million-fold proton gradient across the gastric membrane. We present the structure of gastric H(+),K(+)-ATPase at 6.5 A resolution as determined by electron crystallography of two-dimensional crystals. The structure shows the catalytic alpha-subunit and the non-catalytic beta-subunit in a pseudo-E(2)P conformation. Different from Na(+),K(+)-ATPase, the N-terminal tail of the beta-subunit is in direct contact with the phosphorylation domain of the alpha-subunit. This interaction may hold the phosphorylation domain in place, thus stabilizing the enzyme conformation and preventing the reverse reaction of the transport cycle. Indeed, truncation of the beta-subunit N-terminus allowed the reverse reaction to occur. These results suggest that the beta-subunit N-terminus prevents the reverse reaction from E(2)P to E(1)P, which is likely to be relevant for the generation of a large H(+) gradient in vivo situation.

Indexed as

Cryoelectron MicroscopyGastric MucosaH(+)-K(+)-Exchanging ATPaseModels, MolecularProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein SubunitsSequence DeletionH(+)-K(+)-Exchanging ATPaseProtein Subunits

Identifiers

PMID19387495
PMCPMC2693145
OpenAlexW2104803435

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.