Evidence map›Paper›PMID 31311973›Full record

ArticleScientific reports2019

Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery.

Jyoti Kumari, Rajesh Vinnakota, Janesh Kumar

Open access · greenAbstract readVideo-Audio Media
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Activation of kainate receptor GluK2-Neto2 complex.Nature structural & molecular biology · 2025
    Article
  7. Article
  8. Article
  9. Structure and gating of kainate receptors.Frontiers in pharmacology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Kainate Receptor Antagonists: Recent Advances and Therapeutic Perspective.International journal of molecular sciences · 2023
    Review
  16. Review
  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

3 authors at 1 institution in 1 country.

Jyoti KumariLaboratory of Membrane Protein Biology, National Centre for Cell Science, NCCS Complex, S. P. Pune University, Maharashtra, Pune, 411007, India.
Rajesh VinnakotaLaboratory of Membrane Protein Biology, National Centre for Cell Science, NCCS Complex, S. P. Pune University, Maharashtra, Pune, 411007, India.
Janesh KumarLaboratory of Membrane Protein Biology, National Centre for Cell Science, NCCS Complex, S. P. Pune University, Maharashtra, Pune, 411007, India. janesh@nccs.res.in.
National Centre for Cell Science · IN

Funding

DBT India Alliance (Wellcome Trust/DBT India Alliance) IA/I/13/2/501023Wellcome Trust
6 · The paper itself

Abstract

GluK3-kainate receptors are atypical members of the iGluR family that reside at both the pre- and postsynapse and play a vital role in the regulation of synaptic transmission. For a better understanding of structural changes that underlie receptor functions, GluK3 receptors were trapped in desensitized and resting/closed states and structures analyzed using single particle cryo-electron microscopy. While the desensitized GluK3 has domain organization as seen earlier for another kainate receptor-GluK2, antagonist bound GluK3 trapped a resting state with only two LBD domains in dimeric arrangement necessary for receptor activation. Using structures as a guide, we show that the N-linked glycans at the interface of GluK3 ATD and LBD likely mediate inter-domain interactions and attune receptor-gating properties. The mutational analysis also identified putative N-glycan interacting residues. Our results provide a molecular framework for understanding gating properties unique to GluK3 and exploring the role of N-linked glycosylation in their modulation.

Indexed as

AlanineAnimalsBinding SitesCryoelectron MicroscopyCrystallography, X-RayGluK3 Kainate ReceptorHEK293 CellsHumansKainic Acid ReceptorsMutagenesis, Site-DirectedPolysaccharidesProtein ConformationRatsThymineAlanineGluK3 Kainate ReceptorKainic Acid ReceptorsPolysaccharidesThymineUBP 310

Identifiers

PMID31311973
PMCPMC6635489
OpenAlexW2961517283

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.