Evidence map›Paper›PMID 32962356›Full record

ReviewThe Journal of chemical physics2020

Hydrophobic dewetting in gating and regulation of transmembrane protein ion channels.

Mahdieh Yazdani, Zhiguang Jia, Jianhan Chen

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of chemical physics, 2020. 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
1.6field-weighted citation impact, top 17% 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, 30 citations in OpenAlex.

  1. Article
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  12. Review
  13. When is a hydrophobic gate not a hydrophobic gate?The Journal of general physiology · 2022
    Article
  14. Article
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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 at 1 institution in 1 country.

Mahdieh YazdaniDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.ORCID 0000000313004599
Zhiguang JiaDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Jianhan ChenDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.ORCID 0000000252811150
University of Massachusetts Amherst · US

Funding

Ca2+ Dependent K+ Channels: Allosteric GatingR01HL070393 · NHLBI · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2002 to 2015
$4.9M
Multi-scale enhanced sampling of disordered proteins: Admin Supplement InstrumentationR01GM114300 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHEN, JIANHAN · 2016 to 2020
$1.5M
NHLBI NIH HHS R01 HL070393NIGMS NIH HHS R01 GM114300
6 · The paper itself

Abstract

Water is at the heart of almost all biological phenomena, without which no life that we know of would have been possible. It is a misleadingly complex liquid that exists in near coexistence with the vapor phase under ambient conditions. Confinement within a hydrophobic cavity can tip this balance enough to drive a cooperative dewetting transition. For a nanometer-scale pore, the dewetting transition leads to a stable dry state that is physically open but impermeable to ions. This phenomenon is often referred to as hydrophobic gating. Numerous transmembrane protein ion channels have now been observed to utilize hydrophobic gating in their activation and regulation. Here, we review recent theoretical, simulation, and experimental studies that together have started to establish the principles of hydrophobic gating and discuss how channels of various sizes, topologies, and biological functions can utilize these principles to control the thermodynamic properties of water within their interior pores for gating and regulation. Exciting opportunities remain in multiple areas, particularly on direct experimental detection of hydrophobic dewetting in biological channels and on understanding how the cell may control the hydrophobic gating in regulation of ion channels.

Indexed as

Ion Channel GatingCell MembraneHumansHydrodynamicsIon ChannelsLarge-Conductance Calcium-Activated Potassium ChannelsModels, MolecularNanoporesReceptors, Serotonin, 5-HT3WaterWettabilityIon ChannelsLarge-Conductance Calcium-Activated Potassium ChannelsReceptors, Serotonin, 5-HT3Water

Identifiers

PMID32962356
PMCPMC9722268
OpenAlexW3084786814

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.