Evidence map›Paper›PMID 25556786›Full record

ReviewThe Journal of physiology2015

Assembly of AMPA receptors: mechanisms and regulation.

Quan Gan, Catherine L Salussolia, Lonnie P Wollmuth

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. The effect of traumatic brain injury on learning and memory: A synaptic focus.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2025
    Review
  6. Article
  7. Review
  8. Structure and gating of kainate receptors.Frontiers in pharmacology · 2025
    Review
  9. Review
  10. Review
  11. Allosteric competition and inhibition in AMPA receptors.Nature structural & molecular biology · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. [Tacrolimus Induces Pain by Upregulating the Synaptic Expression of AMPA Receptors in the Spinal Cord Dorsal Horn].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2024
    Article
  16. Epigenetics in rare neurological diseases.Frontiers in cell and developmental biology · 2024
    Review
  17. Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System.International journal of molecular sciences · 2023
    Review
  18. Article
  19. Review
  20. 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

3 authors at 2 institutions in 1 country.

Quan GanGraduate Program in Neuroscience, Stony Brook University, Stony Brook, NY, USA; Center for Nervous System Disorders, Stony Brook University, Stony Brook, NY, USA; Department of Neurobiology and Behaviour, Stony Brook University, Stony Brook, NY, USA.
Catherine L Salussolia
Lonnie P Wollmuth
Stony Brook University · USStony Brook University Hospital · US

Funding

The Functional Significance of Conformational States in Glutamatergic SignalingF31NS073382 · NINDS · STATE UNIVERSITY NEW YORK STONY BROOK · PI SALUSSOLIA, CATHERINE LOURDES · 2011 to 2013
$108k
NINDS NIH HHS NS073382
6 · The paper itself

Abstract

AMPA receptors (AMPARs) play a critical role in excitatory glutamatergic neurotransmission. The number and subunit composition of AMPARs at synapses determines the dynamics of fast glutamatergic signalling. Functional AMPARs on the cell surface are tetramers. Thus tetrameric assembly of AMPARs represents a promising target for modulating AMPAR-mediated signalling in health and disease. Multiple structural domains within the receptor influence AMPAR assembly. In a proposed model for AMPAR assembly, the amino-terminal domain underlies the formation of a dimer pool. The transmembrane domain facilitates the formation and enhances the stability of the tetramer. The ligand-binding domain influences assembly through a process referred to as 'domain swapping'. We propose that this core AMPAR assembly process could be regulated by neuronal signals and speculate on possible mechanisms for such regulation.

Indexed as

Models, MolecularReceptors, AMPAHumansProtein MultimerizationProtein Structure, TertiaryReceptors, AMPA

Identifiers

PMID25556786
PMCPMC4293052
OpenAlexW1600708614

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.