Evidence map›Paper›PMID 30542267›Full record

ArticleFrontiers in cellular neuroscience2018

A Light-Controlled Allosteric Modulator Unveils a Role for mGlu

Simon Bossi, Romain Helleringer, Micaela Galante, Ester Monlleó, Ana Trapero, Xavier Rovira, Hervé Daniel, Amadeu Llebaria, Heather McLean

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cellular neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

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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

9 authors at 5 institutions in 2 countries.

Simon BossiPharmacologie et Biochimie de la Synapse, Institut des Neurosciences Paris-Saclay, Université Paris-Saclay, Université Paris-Sud - CNRS, UMR 9197, Orsay, France.
Romain HelleringerPharmacologie et Biochimie de la Synapse, Institut des Neurosciences Paris-Saclay, Université Paris-Saclay, Université Paris-Sud - CNRS, UMR 9197, Orsay, France.
Micaela GalantePharmacologie et Biochimie de la Synapse, Institut des Neurosciences Paris-Saclay, Université Paris-Saclay, Université Paris-Sud - CNRS, UMR 9197, Orsay, France.
Ester MonlleóMCS, Laboratory of Medicinal Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Barcelona, Spain.
Ana TraperoMCS, Laboratory of Medicinal Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Barcelona, Spain.
Xavier RoviraMolecular Photopharmacology Research Group, The Tissue Repair and Regeneration Laboratory, University of Vic - Central University of Catalonia, Vic, Spain.
Hervé DanielPharmacologie et Biochimie de la Synapse, Institut des Neurosciences Paris-Saclay, Université Paris-Saclay, Université Paris-Sud - CNRS, UMR 9197, Orsay, France.
Amadeu LlebariaMCS, Laboratory of Medicinal Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Barcelona, Spain.
Heather McLeanPharmacologie et Biochimie de la Synapse, Institut des Neurosciences Paris-Saclay, Université Paris-Saclay, Université Paris-Sud - CNRS, UMR 9197, Orsay, France.
Institut des Neurosciences Paris-Saclay · FRInstitute of Advanced Chemistry of Catalonia · ESUniversité Paris-Saclay · FRBiomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine · ESUniversitat de Vic - Universitat Central de Catalunya · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metabotropic glutamate receptors (mGlus) are G Protein coupled-receptors that modulate synaptic transmission and plasticity in the central nervous system. Some act as autoreceptors to control neurotransmitter release at excitatory synapses and have become attractive targets for drug therapy to treat certain neurological disorders. However, the high degree of sequence conservation around the glutamate binding site makes the development of subtype-specific orthosteric ligands difficult to achieve. This problem can be circumvented by designing molecules that target specific less well conserved allosteric sites. One such allosteric drug, the photo-switchable compound OptoGluNAM4.1, has been recently employed to reversibly inhibit the activity of metabotropic glutamate 4 (mGlu

Indexed as

allosteric modulationcerebellar cortexoxygen glucose deprivationphoto-pharmacologypresynaptic metabotropic glutamate receptor 4

Identifiers

PMID30542267
PMCPMC6277836
OpenAlexW2902803614

What OpenQuestion holds

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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.