Evidence map›Paper›PMID 33199909›Full record

ReviewNature chemical biology2020

Ion channels as lipid sensors: from structures to mechanisms.

Mackenzie J Thompson, John E Baenziger

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 70 citations in OpenAlex.

  1. Cholesterol, PtdIns(4,5)PbioRxiv : the preprint server for biology · 2026
    Article
  2. Artificial Nervous Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
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  20. Membranes · 2022
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Mackenzie J ThompsonDepartment of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, Ontario, Canada.ORCID http://orcid.org/0000-0001-8421-4222
John E BaenzigerDepartment of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, Ontario, Canada. John.Baenziger@uottawa.ca.ORCID http://orcid.org/0000-0002-2888-5328
University of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ion channels play critical roles in cellular function by facilitating the flow of ions across the membrane in response to chemical or mechanical stimuli. Ion channels operate in a lipid bilayer, which can modulate or define their function. Recent technical advancements have led to the solution of numerous ion channel structures solubilized in detergent and/or reconstituted into lipid bilayers, thus providing unprecedented insight into the mechanisms underlying ion channel-lipid interactions. Here, we describe how ion channel structures have evolved to respond to both lipid modulators and lipid activators to control the electrical activities of cells, highlighting diverse mechanisms and common themes.

Indexed as

AnimalsBinding SitesCell CommunicationCell MembraneEukaryotic CellsG Protein-Coupled Inwardly-Rectifying Potassium ChannelsHumansLipid BilayersMammalsModels, MolecularPhosphatidylinositol PhosphatesPotassium Channels, Tandem Pore DomainPotassium Channels, Voltage-GatedProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandG Protein-Coupled Inwardly-Rectifying Potassium ChannelsLipid BilayersPhosphatidylinositol PhosphatesPotassium Channels, Tandem Pore DomainPotassium Channels, Voltage-Gated

Identifiers

PMID33199909
OpenAlexW3103439995

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.