Evidence map›Paper›PMID 21080238›Full record

ReviewMolecular neurobiology2010

The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors.

Terunaga Nakagawa

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular neurobiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. AMPA receptor structure and auxiliary subunits.The Journal of physiology · 2021
    Review
  8. Article
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  10. Article
  11. Review
  12. Article
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  15. Review
  16. Review
  17. Review
  18. Article
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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

1 author at 1 institution in 1 country.

Terunaga NakagawaDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA. nakagawa@ucsd.edu
University of California, San Diego · US

Funding

Molecular Anatomy of Mature and Immature Glutamate ReceptorsR01HD061543 · NICHD · VANDERBILT UNIVERSITY · PI NAKAGAWA, TERUNAGA · 2010 to 2014
$1.5M
NICHD NIH HHS R01 HD061543NICHD NIH HHS R01HD061543
6 · The paper itself

Abstract

The AMPA-type ionotropic glutamate receptors (AMPA-Rs) are tetrameric ligand-gated ion channels that play crucial roles in synaptic transmission and plasticity. Our knowledge about the ultrastructure and subunit assembly mechanisms of intact AMPA-Rs was very limited. However, the new studies using single particle EM and X-ray crystallography are revealing important insights. For example, the tetrameric crystal structure of the GluA2cryst construct provided the atomic view of the intact receptor. In addition, the single particle EM structures of the subunit assembly intermediates revealed the conformational requirement for the dimer-to-tetramer transition during the maturation of AMPA-Rs. These new data in the field provide new models and interpretations. In the brain, the native AMPA-R complexes contain auxiliary subunits that influence subunit assembly, gating, and trafficking of the AMPA-Rs. Understanding the mechanisms of the auxiliary subunits will become increasingly important to precisely describe the function of AMPA-Rs in the brain. The AMPA-R proteomics studies continuously reveal a previously unexpected degree of molecular heterogeneity of the complex. Because the AMPA-Rs are important drug targets for treating various neurological and psychiatric diseases, it is likely that these new native complexes will require detailed mechanistic analysis in the future. The current ultrastructural data on the receptors and the receptor-expressing stable cell lines that were developed during the course of these studies are useful resources for high throughput drug screening and further drug designing. Moreover, we are getting closer to understanding the precise mechanisms of AMPA-R-mediated synaptic plasticity.

Indexed as

Protein Conformationalpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidAnimalsBrainCell LineCrystallography, X-RayDimerizationExcitatory Amino Acid AntagonistsGlutamic AcidHumansModels, MolecularProtein SubunitsQuinoxalinesReceptors, AMPA2,3-dioxo-6-nitro-7-sulfamoylbenzo(f)quinoxalinealpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidExcitatory Amino Acid AntagonistsGlutamic AcidProtein SubunitsQuinoxalinesReceptors, AMPA

Identifiers

PMID21080238
PMCPMC2992128
OpenAlexW2135999567

What OpenQuestion holds

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LicenceCC BY-NC
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.