Evidence map›Paper›PMID 19883588›Full record

ArticleBiophysical journal2009

Gating transition of pentameric ligand-gated ion channels.

Fangqiang Zhu, Gerhard Hummer

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Gating mechanism of a P2X4 receptor developed from normal mode analysis and molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Vinculin motion modes analysis with elastic network model.International journal of molecular sciences · 2012
    Article
  13. Review
  14. Article
  15. Pore opening and closing of a pentameric ligand-gated ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  16. One-microsecond molecular dynamics simulation of channel gating in a nicotinic receptor homologue.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  17. Article
  18. 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 at 2 institutions in 1 country.

Fangqiang ZhuLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Gerhard Hummer
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Water, protons, and ions biomolecular systemsZIADK029036 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2009 to 2012
$1.9M
Intramural NIH HHS
6 · The paper itself

Abstract

Pentameric ligand-gated ion channels are an important family of membrane proteins and play key roles in physiological processes, including signal transduction at chemical synapses. Here, we study the conformational changes associated with the opening and closing of the channel pore. Based on recent crystal structures of two prokaryotic members of the family in open and closed states, respectively, mixed elastic network models are constructed for the transmembrane domain. To explore the conformational changes in the gating transition, a coarse-grained transition path is computed that smoothly connects the closed and open conformations of the channel. We find that the conformational transition involves no major rotations of the transmembrane helices, and is instead characterized by a concerted tilting of helices M2 and M3. In addition, helix M2 changes its bending state, which results in an early closure of the pore during the open-to-closed transition.

Indexed as

Ion Channel GatingBacterial ProteinsBiophysicsCell MembraneComputer SimulationElasticityElectrophysiologyIon ChannelsLigandsMembrane ProteinsModels, StatisticalMolecular ConformationProtein BindingProtein ConformationBacterial ProteinsIon ChannelsLigandsMembrane Proteins

Identifiers

PMID19883588
PMCPMC2770624
OpenAlexW2166138676

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.