Evidence map›Paper›PMID 19486673›Full record

ArticleBiophysical journal2009

Molecular-dynamics simulations of ELIC-a prokaryotic homologue of the nicotinic acetylcholine receptor.

Xiaolin Cheng, Ivaylo Ivanov, Hailong Wang, Steven M Sine, J Andrew McCammon

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. The nicotinic acetylcholine receptor: a typical 'allosteric machine'.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  5. Article
  6. Article
  7. Article
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  9. Article
  10. Article
  11. Review
  12. A gating mechanism of pentameric ligand-gated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. An Update on GABAρ Receptors.Current neuropharmacology · 2010
    Article
  20. 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
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

5 authors at 3 institutions in 1 country.

Xiaolin ChengCenter for Molecular Biophysics, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA. xcheng@mccammon.ucsd.edu
Ivaylo Ivanov
Hailong Wang
Steven M Sine
J Andrew McCammon
Mayo Clinic · USU.S. National Science Foundation · USOak Ridge National Laboratory · US

Funding

THEORY OF BIOMOLECULAR DIFFUSIONR01GM031749 · NIGMS · UNIVERSITY OF HOUSTON · PI HUBER, GARY ALEXANDER, MCCAMMON, JAMES ANDREW · 1985 to 2022
$7.8M
STRUCTURE/FUNCTION OF THE ACETYLCHOLINE RECEPTORR01NS031744 · NINDS · MAYO CLINIC ROCHESTER · PI SINE, STEVEN M · 1992 to 2023
$7.3M
Howard Hughes Medical InstituteNIGMS NIH HHS GM31749NIGMS NIH HHS R01 GM031749NINDS NIH HHS R01 NS031744
6 · The paper itself

Abstract

The ligand-gated ion channel from Erwinia chrysanthemi (ELIC) is a prokaryotic homolog of the eukaryotic nicotinic acetylcholine receptor (nAChR) that responds to the binding of neurotransmitter acetylcholine and mediates fast signal transmission. ELIC is similar to the nAChR in its primary sequence and overall subunit organization, but despite their structural similarity, it is not clear whether these two ligand-gated ion channels operate in a similar manner. Further, it is not known to what extent mechanistic insights gleaned from the ELIC structure translate to eukaryotic counterparts such as the nAChR. Here we use molecular-dynamics simulations to probe the conformational dynamics and hydration of the transmembrane pore of ELIC. The results are compared with those from our previous simulation of the human alpha7 nAChR. Overall, ELIC displays increased stability compared to the nAChR, whereas the two proteins exhibit remarkable similarity in their global motion and flexibility patterns. The majority of the increased stability of ELIC does not stem from the deficiency of the models used in the simulations, and but rather seems to have a structural basis. Slightly altered dynamical correlation features are also observed among several loops within the membrane region. In sharp contrast to the nAChR, ELIC is completely dehydrated from the pore center to the extracellular end throughout the simulation. Finally, the simulation of an ELIC mutant substantiates the important role of F246 on the stability, hydration and possibly function of the ELIC channel.

Indexed as

Computer SimulationModels, Chemicalalpha7 Nicotinic Acetylcholine ReceptorAmino Acid SequenceBacterial ProteinsDickeya chrysanthemiElasticityHumansIon ChannelsLipid BilayersModels, MolecularMotionMutationProtein ConformationProtein StabilityReceptors, Nicotinicalpha7 Nicotinic Acetylcholine ReceptorBacterial ProteinsChrna7 protein, humanIon ChannelsLipid BilayersReceptors, NicotinicWater

Identifiers

PMID19486673
PMCPMC2711484
OpenAlexW2074698050

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.