Evidence map›Paper›PMID 41625315›Full record

ArticleBiochemistry (Moscow) Supplement. Series A, Membrane and cell biology2022

Structural insights into function of ionotropic glutamate receptors.

Maria V Yelshanskaya, Alexander I Sobolevsky

Abstract read
In one paragraph

Article in Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Activation of kainate receptor GluK2-Neto2 complex.Nature structural & molecular biology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Review
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.

Maria V YelshanskayaDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

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
Single-Particle Cryo-EM Characterization of AMPA Receptor Functional StatesR01NS107253 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2018 to 2026
$3.5M
NCI NIH HHS R01 CA206573NINDS NIH HHS R01 NS083660NINDS NIH HHS R01 NS107253
6 · The paper itself

Abstract

Ionotropic glutamate receptors (iGluRs) mediate fast excitatory neurotransmission. They are implicated in nervous system development and function, while their dysfunction is associated with neurological and psychiatric disorders. In this review, we describe recent progress in structural studies of iGluRs and how crystal and cryo-EM structures helped determining the principles of iGluR architecture and assembly, and the mechanisms of activation, desensitization and regulation by auxiliary subunits, positive and negative allosteric modulators, and ion channel blockers. The new structural insights facilitate better understanding of iGluR physiological and pathophysiological roles in functioning of the central nervous system and provide valuable information for structure-based drug design.

Indexed as

AMPA receptorauxiliary subunitchannel blockercryo-EMdelta receptordesensitizationgatingGLRiGluRinhibitorkainate receptorNMDA receptorX-ray crystallography

Identifiers

PMID41625315
PMCPMC12860490

What OpenQuestion holds

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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.