Evidence map›Paper›PMID 19597538›Full record

ArticlePLoS biology2009

Inherent dynamics of the acid-sensing ion channel 1 correlates with the gating mechanism.

Huaiyu Yang, Ye Yu, Wei-Guang Li, Fang Yu, Hui Cao, Tian-Le Xu, Hualiang Jiang

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 68 citations in OpenAlex.

  1. Conformational plasticity of human acid-sensing ion channel 1a.Nature structural & molecular biology · 2026
    Article
  2. Article
  3. Epithelial NaComprehensive Physiology · 2024
    Review
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  11. Acid-sensing ion channels emerged over 600 Mya and are conserved throughout the deuterostomes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Human ASIC1a mediates stronger acid-induced responses as compared with mouse ASIC1a.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
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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

7 authors at 2 institutions in 1 country.

Huaiyu YangDrug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Ye Yu
Wei-Guang Li
Fang Yu
Hui Cao
Tian-Le Xu
Hualiang Jiang
Chinese Academy of Sciences · CNShanghai Institutes for Biological Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The acid-sensing ion channel 1 (ASIC1) is a key receptor for extracellular protons. Although numerous structural and functional studies have been performed on this channel, the structural dynamics underlying the gating mechanism remains unknown. We used normal mode analysis, mutagenesis, and electrophysiological methods to explore the relationship between the inherent dynamics of ASIC1 and its gating mechanism. Here we show that a series of collective motions among the domains and subdomains of ASIC1 correlate with its acid-sensing function. The normal mode analysis result reveals that the intrinsic rotation of the extracellular domain and the collective motions between the thumb and finger induced by proton binding drive the receptor to experience a deformation from the extracellular domain to the transmembrane domain, triggering the channel pore to undergo "twist-to-open" motions. The movements in the transmembrane domain indicate that the likely position of the channel gate is around Leu440. These motion modes are compatible with a wide body of our complementary mutations and electrophysiological data. This study provides the dynamic fundamentals of ASIC1 gating.

Indexed as

Ion Channel GatingAcid Sensing Ion ChannelsAmino Acid SequenceAnimalsCHO CellsComputer SimulationCricetinaeCricetulusDNA, ComplementaryHumansModels, ChemicalMolecular Sequence DataMotionMutagenesis, Site-DirectedNerve Tissue ProteinsProtein Structure, TertiaryAcid Sensing Ion ChannelsASIC1 protein, humanDNA, ComplementaryNerve Tissue ProteinsSodium Channels

Identifiers

PMID19597538
PMCPMC2701601
OpenAlexW2057602646

What OpenQuestion holds

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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.