Evidence map›Paper›PMID 28432359›Full record

ArticleScientific reports2017

Role of the Ion Channel Extracellular Collar in AMPA Receptor Gating.

Maria V Yelshanskaya, Samaneh Mesbahi-Vasey, Maria G Kurnikova, Alexander I Sobolevsky

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

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  14. Molecular dysregulation of ciliary polycystin-2 channels caused by variants in the TOP domain.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
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  18. Distinct roles ofF1000Research · 2019
    Review
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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

4 authors at 2 institutions in 1 country.

Maria V YelshanskayaDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY, 10032, USA.
Samaneh Mesbahi-VaseyChemistry Department, Carnegie Mellon University, 4400 Fifth Ave, Pittsburgh, PA, 15213, USA.
Maria G KurnikovaChemistry Department, Carnegie Mellon University, 4400 Fifth Ave, Pittsburgh, PA, 15213, USA. kurnikova@cmu.edu.
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY, 10032, USA. as4005@cumc.columbia.edu.
Carnegie Mellon University · USColumbia University · US

Funding

Structure and Function of AMPA subtype ionotropic glutamate receptorsR01NS083660 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI KURNIKOVA, MARIA G, SOBOLEVSKY, ALEXANDER · 2013 to 2022
$4.3M
Structure and function of Transient Receptor Potential ChannelsR01CA206573 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2017 to 2026
$3.8M
Approaches to Modeling Key Elements in Glutamate Receptors Activation MechanismR21NS074267 · NINDS · CARNEGIE-MELLON UNIVERSITY · PI KURNIKOVA, MARIA G · 2011 to 2012
$415k
NCI NIH HHS R01 CA206573NINDS NIH HHS R01 NS083660NINDS NIH HHS R21 NS074267
6 · The paper itself

Abstract

AMPA subtype ionotropic glutamate receptors mediate fast excitatory neurotransmission and are implicated in numerous neurological diseases. Ionic currents through AMPA receptor channels can be allosterically regulated via different sites on the receptor protein. We used site-directed mutagenesis and patch-clamp recordings to probe the ion channel extracellular collar, the binding region for noncompetitive allosteric inhibitors. We found position and substitution-dependent effects for introduced mutations at this region on AMPA receptor gating. The results of mutagenesis suggested that the transmembrane domains M1, M3 and M4, which contribute to the ion channel extracellular collar, undergo significant relative displacement during gating. We used molecular dynamics simulations to predict an AMPA receptor open state structure and rationalize the results of mutagenesis. We conclude that the ion channel extracellular collar plays a distinct role in gating and represents a hub for powerful allosteric modulation of AMPA receptor function that can be used for developing novel therapeutics.

Identifiers

PMID28432359
PMCPMC5430913
OpenAlexW2605514275

What OpenQuestion holds

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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.