Evidence map›Paper›PMID 28883437›Full record

ArticleScientific reports2017

Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers.

A Patrizio, M Renner, R Pizzarelli, A Triller, C G Specht

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  5. Gating mechanism of the human α1β GlyR by glycine.Structure (London, England : 1993) · 2024
    Article
  6. Modular Structure and Polymerization Status of GABAInternational journal of molecular sciences · 2024
    Article
  7. Role of the Glycine Receptor β Subunit in Synaptic Localization and Pathogenicity in Severe Startle Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    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

5 authors at 2 institutions in 1 country.

A PatrizioÉcole Normale Supérieure, PSL Research University, CNRS, Inserm, Institute of Biology (IBENS), Paris, 75005, France.
M RennerUniversité Pierre et Marie Curie, Institut du Fer à Moulin (IFM), Paris, 75005, France.
R PizzarelliÉcole Normale Supérieure, PSL Research University, CNRS, Inserm, Institute of Biology (IBENS), Paris, 75005, France.
A TrillerÉcole Normale Supérieure, PSL Research University, CNRS, Inserm, Institute of Biology (IBENS), Paris, 75005, France.
C G SpechtÉcole Normale Supérieure, PSL Research University, CNRS, Inserm, Institute of Biology (IBENS), Paris, 75005, France. specht@biologie.ens.fr.ORCID 0000-0001-6038-7735
Centre National de la Recherche Scientifique · FRInstitut du Fer à Moulin · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulation of glycine receptors at synapses requires the interaction between the beta subunit of the receptor and the scaffold protein gephyrin. Here, we questioned whether different alpha subunits could modulate the receptors' diffusion and propensity to cluster at spinal cord synapses. Using quantitative photoactivated localisation microscopy we found that alpha-1 and alpha-3 containing glycine receptors display the same α

Indexed as

Gene Expression RegulationAnimalsCarrier ProteinsChlorocebus aethiopsCOS CellsHumansMembrane ProteinsProtein BindingProtein MultimerizationRatsReceptors, GlycineSynapsesCarrier ProteinsgephyrinMembrane ProteinsReceptors, Glycine

Identifiers

PMID28883437
PMCPMC5589798
OpenAlexW2752141406

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.