Evidence map›Paper›PMID 33355710›Full record

ArticleEuropean biophysics journal : EBJ2021

Lipid-protein forces predict conformational changes in a mechanosensitive channel.

Csaba Daday, Bert L de Groot

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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

2 authors.

Csaba DadayDepartment of Theoretical and Computational Biophysics, Computational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Bert L de GrootDepartment of Theoretical and Computational Biophysics, Computational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. bgroot@gwdg.de.ORCID http://orcid.org/0000-0003-3570-3534

Funding

Deutsche Forschungsgemeinschaft SFB803 A03
6 · The paper itself

Abstract

The mechanosensitive TREK-2 potassium channel, a member of the K2P family, has essential physiological roles and is, therefore, a pharmaceutical target. A combination of experimental and computational studies have established that of the two known conformations, "up" and "down", membrane tension directly favors the "up" state, which displays a higher conductance. However, these studies did not reveal the exact mechanism by which the membrane affects the channel conformation. In this work, we show that changes in protein-lipid interaction patterns suffice in predicting this conformational change, and pinpoint potentially important residues involved in this phenomenon.

Indexed as

Potassium Channels, Tandem Pore DomainProtein ConformationBiomechanical PhenomenaMechanotransduction, CellularMolecular Dynamics SimulationProtein BindingPotassium Channels, Tandem Pore DomainConformational changeForce distribution analysisFunctional mode analysisIon channelMembrane tension

Identifiers

PMID33355710
PMCPMC8071793

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Registered trials

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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.