Evidence map›Paper›PMID 36441147›Full record

ReviewThe Journal of general physiology2023

Mechanistic insights on KATP channel regulation from cryo-EM structures.

Camden M Driggers, Show-Ling Shyng

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of general physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.0field-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

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. A fluorescent probe for the enzymatic activity of KbioRxiv : the preprint server for biology · 2025
    Article
  6. Bayliss-Starling Prize Lecture: KThe Journal of physiology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Dynamic duo: Kir6 and SUR in KChannels (Austin, Tex.) · 2024
    Review
  14. Article
  15. Structure of an open KNature communications · 2024
    Article
  16. Review
  17. KCurrent opinion in structural biology · 2023
    Review
  18. Article
  19. CL-705G: a novel chemical Kir6.2-specific KFrontiers in pharmacology · 2023
    Article
  20. KFrontiers in endocrinology · 2023
    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

2 authors at 1 institution in 1 country.

Camden M DriggersDepartment of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR.ORCID 0000-0002-2105-7175
Show-Ling ShyngDepartment of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR.ORCID 0000-0002-8230-8820
Oregon Health & Science University · US

Funding

Structural Basis of KATP Channel GatingR01DK066485 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SHYNG, SHOW-LING · 2006 to 2024
$5.8M
Correlating structure and function in KATP channel isoformsR01GM145784 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI SHYNG, SHOW-LING · 2022 to 2025
$1.5M
NIDDK NIH HHS R01 DK066485NIGMS NIH HHS R01 GM145784NIH HHS DK066485
6 · The paper itself

Abstract

Gated by intracellular ATP and ADP, ATP-sensitive potassium (KATP) channels couple cell energetics with membrane excitability in many cell types, enabling them to control a wide range of physiological processes based on metabolic demands. The KATP channel is a complex of four potassium channel subunits from the Kir channel family, Kir6.1 or Kir6.2, and four sulfonylurea receptor subunits, SUR1, SUR2A, or SUR2B, from the ATP-binding cassette (ABC) transporter family. Dysfunction of KATP channels underlies several human diseases. The importance of these channels in human health and disease has made them attractive drug targets. How the channel subunits interact with one another and how the ligands interact with the channel to regulate channel activity have been long-standing questions in the field. In the past 5 yr, a steady stream of high-resolution KATP channel structures has been published using single-particle cryo-electron microscopy (cryo-EM). Here, we review the advances these structures bring to our understanding of channel regulation by physiological and pharmacological ligands.

Indexed as

Adenosine TriphosphateKATP ChannelsCryoelectron MicroscopyHumansLigandsSulfonylurea ReceptorsAdenosine TriphosphateKATP ChannelsLigandsSulfonylurea Receptors

Identifiers

PMID36441147
PMCPMC9700523
OpenAlexW4310075648

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.