ReviewNature reviews. Neuroscience2012
Dancing partners at the synapse: auxiliary subunits that shape kainate receptor function.
Review in Nature reviews. Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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.
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.
Who cites it
60 citing papers in PubMed, 96 citations in OpenAlex.
- Cryo-EM structures of apo, agonist- and antagonist-bound heteromeric kainate receptors.Science advances · 2026Article
- Multilayered regulation of GluK3 kainate receptors is mediated by Neto subunits and zinc.Communications biology · 2026Article
- Structural insights into kainate receptor desensitization.Nature communications · 2025Article
- Multilayer control of KaiR1D-autoreceptor function by the auxiliary protein Neto.bioRxiv : the preprint server for biology · 2025Article
- Targeting NETO2 suppresses cell proliferation, invasion, and migration and inactivates the STAT3/C-MYC pathway in hepatocellular carcinoma.World journal of surgical oncology · 2025Article
- α5-nAChR/NETO2 contributed to chronic stress-promoted lung adenocarcinoma progression.Cancer cell international · 2025Article
- Structure and gating of kainate receptors.Frontiers in pharmacology · 2025Review
- Trapping of spermine, Kukoamine A, and polyamine toxin blockers in GluK2 kainate receptor channels.Nature communications · 2024Article
- GluK2 Q/R editing regulates kainate receptor signaling and long-term potentiation of AMPA receptors.iScience · 2023Article
- NETO2 promotes melanoma progression via activation of the CaFrontiers of medicine · 2023Article
- Article
- Kainate receptor modulation by NETO2.Nature · 2021Article
- Structural and compositional diversity in the kainate receptor family.Cell reports · 2021Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Clustered mutations in the GRIK2 kainate receptor subunit gene underlie diverse neurodevelopmental disorders.American journal of human genetics · 2021Article
- Interplay between Gating and Block of Ligand-Gated Ion Channels.Brain sciences · 2020Review
- The auxiliary glutamate receptor subunit dSol-1 promotes presynaptic neurotransmitter release and homeostatic potentiation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3.The EMBO journal · 2020Article
- Neto-α Controls Synapse Organization and Homeostasis at the Drosophila Neuromuscular Junction.Cell reports · 2020Article
- Neto proteins regulate gating of the kainate-type glutamate receptor GluK2 through two binding sites.The Journal of biological chemistry · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kainate receptors are a family of ionotropic glutamate receptors whose physiological roles differ from those of other subtypes of glutamate receptors in that they predominantly serve as modulators, rather than mediators, of synaptic transmission. Neuronal kainate receptors exhibit unusually slow kinetic properties that have been difficult to reconcile with the behaviour of recombinant kainate receptors. Recently, however, the neuropilin and tolloid-like 1 (NETO1) and NETO2 proteins were identified as auxiliary kainate receptor subunits that shape both the biophysical properties and synaptic localization of these receptors.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.