Evidence map›Paper›PMID 29037031›Full record

ArticleBiochemistry2018

Structural Mechanisms of Gating in Ionotropic Glutamate Receptors.

Edward C Twomey, Alexander I Sobolevsky

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

77 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. GluDs are ionotropic dopamine receptors tuned by G-proteins.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Activation of kainate receptor GluK2-Neto2 complex.Nature structural & molecular biology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Allosteric competition and inhibition in AMPA receptors.Nature structural & molecular biology · 2024
    Article
  19. Temperature Sensitive Glutamate Gating of AMPA-subtype iGluRs.bioRxiv : the preprint server for biology · 2024
    Article
  20. Review

17 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Edward C TwomeyDepartment of Biochemistry and Molecular Biophysics and ‡Integrated Program in Cellular, Molecular, and Biomedical Studies, Columbia University , 650 West 168th Street, New York, New York 10032, United States.ORCID 0000-0002-1855-1586
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics and ‡Integrated Program in Cellular, Molecular, and Biomedical Studies, Columbia University , 650 West 168th Street, New York, New York 10032, United States.ORCID 0000-0001-5181-8644
Columbia University · US

Funding

TRAINING IN CELLULAR, MOLECULAR AND BIOPHYSICAL STUDIEST32GM008224 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI LIEM, RONALD K. · 1987 to 2021
$9.9M
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
Structural elucidation of ionotropic glutamate receptor states with cryoelectron microscopyF31NS093838 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI TWOMEY, EDWARD C · 2016 to 2017
$84k
NCI NIH HHS R01 CA206573NIGMS NIH HHS T32 GM008224NINDS NIH HHS F31 NS093838NINDS NIH HHS R01 NS083660
6 · The paper itself

Abstract

Ionotropic glutamate receptors (iGluRs) are ligand-gated ion channels that mediate the majority of excitatory neurotransmission in the central nervous system. iGluRs open their ion channels in response to binding of the neurotransmitter glutamate, rapidly depolarize the postsynaptic neuronal membrane, and initiate signal transduction. Recent studies using X-ray crystallography and cryo-electron microscopy have determined full-length iGluR structures that (1) uncover the receptor architecture in an unliganded, resting state, (2) reveal conformational changes produced by ligands in order to activate iGluRs, open their ion channels, and conduct ions, and (3) show how activated, glutamate-bound iGluRs can adopt a nonconducting desensitized state. These new findings, combined with the results of previous structural and functional experiments, kinetic and molecular modeling, mutagenesis, and biochemical analyses, provide new views on the structural mechanisms of iGluR gating.

Indexed as

Ion Channel GatingCryoelectron MicroscopyCrystallography, X-RayHumansLigandsProtein ConformationReceptors, AMPALigandsReceptors, AMPA

Identifiers

PMID29037031
PMCPMC5780838
OpenAlexW2766528848

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.