Evidence map›Paper›PMID 31628192›Full record

ArticleThe Journal of biological chemistry2019

Neto proteins regulate gating of the kainate-type glutamate receptor GluK2 through two binding sites.

Yan-Jun Li, Gui-Fang Duan, Jia-Hui Sun, Dan Wu, Chang Ye, Yan-Yu Zang, Gui-Quan Chen, Yong-Yun Shi, Jun Wang, Wei Zhang and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Activation of kainate receptor GluK2-Neto2 complex.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Structure and gating of kainate receptors.Frontiers in pharmacology · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. 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

11 authors at 5 institutions in 1 country.

Yan-Jun LiState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China.
Gui-Fang DuanState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China.
Jia-Hui SunState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China.
Dan WuState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China.
Chang YeState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China.
Yan-Yu ZangState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China.
Gui-Quan ChenState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China.
Yong-Yun ShiDepartment of Orthopaedics, Luhe People's Hospital Affiliated to Yangzhou University, Nanjing 211500, China.
Jun WangMinistry of Education Key Laboratory of Modern Toxicology, Department of Toxicology, School of Public Health, Nanjing Medical University, Nanjing 211166, China.
Wei ZhangInstitute of Chinese Integrative Medicine, Hebei Medical University, Shijiazhuang 050017, China weizhang@hebmu.edu.cn.
Yun Stone ShiState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, and Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing 210032, China yunshi@nju.edu.cn.
Model Animal Research Center · CNNanjing University · CNHebei Medical University · CNNanjing Medical University · CNYangzhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neuropilin and tolloid-like (Neto) proteins Neto1 and Neto2 are auxiliary subunits of kainate-type glutamate receptors (KARs) that regulate KAR trafficking and gating. However, how Netos bind and regulate the biophysical functions of KARs remains unclear. Here, we found that the N-terminal domain (NTD) of glutamate receptor ionotropic kainate 2 (GluK2) binds the first complement C1r/C1s-Uegf-BMP (CUB) domain of Neto proteins (

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsBinding SitesGluK2 Kainate ReceptorHEK293 CellsHumansKainic Acid ReceptorsMembrane ProteinsMiceModels, BiologicalModels, MolecularProtein BindingProtein DomainsRatsReceptors, N-Methyl-D-AspartateGluK2 Kainate ReceptorKainic Acid ReceptorsMembrane ProteinsNeto1 protein, mouseNeto2 protein, ratReceptors, N-Methyl-D-Aspartateallosteric regulationchannel gatingCUB domaindeactivationdesensitizationgatingglutamate ionotropic receptor kainate type subunit 2 (GriK2)glutamate receptor ionotropic kainate 2 (GluK2)ionotropic glutamate receptorkainate receptorneuropilin and tolloid-like (Neto)N-terminal domain (NTD)protein-protein interactionreceptor desensitizationrecovery from desensitization

Identifiers

PMID31628192
PMCPMC6879349
OpenAlexW2981113386

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.