Evidence map›Paper›PMID 35596528›Full record

ArticleBiophysical journal2022

Transition between conformational states of the TREK-1 K2P channel promoted by interaction with PIP

Adisorn Panasawatwong, Tanadet Pipatpolkai, Stephen J Tucker

Abstract read
In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. The potassium channel KNature communications · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Alchemical Free Energy Calculations on Membrane-Associated Proteins.Journal of chemical theory and computation · 2023
    Review
  8. 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.

Adisorn PanasawatwongDepartment of Physics, University of Oxford, Oxford, United Kingdom.
Tanadet PipatpolkaiDepartment of Physiology Anatomy and Genetics, University of Oxford, Oxford, United Kingdom; Department of Biochemistry, University of Oxford, Oxford, United Kingdom; OXION Initiative in Ion Channels and Disease, University of Oxford, Oxford, United Kingdom. Electronic address: tanadet.pipatpolkai@scilifelab.se.
Stephen J TuckerDepartment of Physics, University of Oxford, Oxford, United Kingdom; OXION Initiative in Ion Channels and Disease, University of Oxford, Oxford, United Kingdom; Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford, United Kingdom. Electronic address: stephen.tucker@physics.ox.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the TREK family of two-pore domain potassium channels are highly sensitive to regulation by membrane lipids, including phosphatidylinositol-4,5-bisphosphate (PIP

Indexed as

Potassium Channels, Tandem Pore DomainBinding SitesMolecular ConformationMolecular Dynamics SimulationPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol 4,5-Diphosphatepotassium channel protein TREK-1Potassium Channels, Tandem Pore Domain

Identifiers

PMID35596528
PMCPMC9279171

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.