Evidence map›Paper›PMID 23955023›Full record

ArticleNature structural & molecular biology2013

Defining the structural relationship between kainate-receptor deactivation and desensitization.

G Brent Dawe, Maria Musgaard, Elizabeth D Andrews, Bryan A Daniels, Mark R P Aurousseau, Philip C Biggin, Derek Bowie

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

32 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structure and gating of kainate receptors.Frontiers in pharmacology · 2025
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Subunit-selective iGluR antagonists can potentiate heteromeric receptor responses by blocking desensitization.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  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

7 authors at 2 institutions in 2 countries.

G Brent Dawe1] Integrated Program in Neuroscience, McGill University, Montréal, Québec, Canada. [2] Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada. [3].
Maria Musgaard
Elizabeth D Andrews
Bryan A Daniels
Mark R P Aurousseau
Philip C Biggin
Derek Bowie
McGill University · CAUniversity of Oxford · GB

Funding

CIHR 82804-1CIHR FRN-82804
6 · The paper itself

Abstract

Desensitization is an important mechanism curtailing the activity of ligand-gated ion channels (LGICs). Although the structural basis of desensitization is not fully resolved, it is thought to be governed by physicochemical properties of bound ligands. Here, we show the importance of an allosteric cation-binding pocket in controlling transitions between activated and desensitized states of rat kainate-type (KAR) ionotropic glutamate receptors (iGluRs). Tethering a positive charge to this pocket sustains KAR activation, preventing desensitization, whereas mutations that disrupt cation binding eliminate channel gating. These different outcomes explain the structural distinction between deactivation and desensitization. Deactivation occurs when the ligand unbinds before the cation, whereas desensitization proceeds if a ligand is bound without cation pocket occupancy. This sequence of events is absent from AMPA-type iGluRs; thus, cations are identified as gatekeepers of KAR gating, a role unique among even closely related LGICs.

Indexed as

AnimalsBinding SitesGluK2 Kainate ReceptorHEK293 CellsHumansIon Channel GatingKainic Acid ReceptorsLigandsModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein MultimerizationProtein SubunitsRatsReceptors, AMPARecombinant ProteinsGluK2 Kainate ReceptorKainic Acid ReceptorsLigandsProtein SubunitsReceptors, AMPARecombinant Proteins

Identifiers

PMID23955023
PMCPMC4972573
OpenAlexW2053680372

What OpenQuestion holds

Textmetadata
LicenceTDM
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.