Evidence map›Paper›PMID 26682803›Full record

ReviewBiophysical journal2015

The Nucleotide-Binding Sites of SUR1: A Mechanistic Model.

Natascia Vedovato, Frances M Ashcroft, Michael C Puljung

Abstract readReview
In one paragraph

Review in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. A fluorescent probe for the enzymatic activity of KbioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Article
  4. CatSper Calcium Channels: 20 Years On.Physiology (Bethesda, Md.) · 2023
    Review
  5. Article
  6. Article
  7. Molecular structure of an open human KProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. The expression of KAnnals of translational medicine · 2018
    Article
  16. 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.

Natascia VedovatoDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford, United Kingdom.
Frances M AshcroftDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford, United Kingdom.
Michael C PuljungDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford, United Kingdom. Electronic address: michael.puljung@dpag.ox.ac.uk.

Funding

Wellcome TrustWellcome Trust 089795
6 · The paper itself

Abstract

ATP-sensitive potassium (KATP) channels comprise four pore-forming Kir6.2 subunits and four modulatory sulfonylurea receptor (SUR) subunits. The latter belong to the ATP-binding cassette family of transporters. KATP channels are inhibited by ATP (or ADP) binding to Kir6.2 and activated by Mg-nucleotide interactions with SUR. This dual regulation enables the KATP channel to couple the metabolic state of a cell to its electrical excitability and is crucial for the KATP channel's role in regulating insulin secretion, cardiac and neuronal excitability, and vascular tone. Here, we review the regulation of the KATP channel by adenine nucleotides and present an equilibrium allosteric model for nucleotide activation and inhibition. The model can account for many experimental observations in the literature and provides testable predictions for future experiments.

Indexed as

Models, MolecularBinding SitesIon Channel GatingNucleotidesProtein Structure, TertiarySulfonylurea ReceptorsNucleotidesSulfonylurea Receptors

Identifiers

PMID26682803
PMCPMC4699857

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.