Evidence map›Paper›PMID 12392061›Full record

ReviewMolecular neurobiology2002

Targeted trafficking of neurotransmitter receptors to synaptic sites.

Sophie Marchand, Jean Cartaud

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2002. 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
0.6field-weighted citation impact, top 39% 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, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Intracellular association of glycine receptor with gephyrin increases its plasma membrane accumulation rate.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    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

2 authors at 2 institutions in 1 country.

Sophie MarchandBiologie Cellulaire des Membranes, Institut Jacques Monod, UMR 7592, CNRS/Université Paris 6, France.
Jean Cartaud
Institut Jacques Monod · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Emerging data are sheding light on the critical task for synapses to locally control the production of neurotransmitter receptors ultimately leading to receptor accumulation and modulation at postsynaptic sites. By analogy with the epithelial-cell paradigm, the postsynaptic compartment may be regarded as a polarized domain favoring the selective recruitment and retention of newly delivered receptors at synaptic sites. Targeted delivery of receptors to synaptic sites is facilitated by a local organization of the exocytic pathway, likely resulting from spatial cues triggered by the nerve. This review focuses on the various mechanisms responsible for regulation of receptor assembly and trafficking. A particular emphasis is given to the role of synaptic anchoring and scaffolding proteins in the sorting and routing of their receptor companion along the exocytic pathway. Other cellular components such as lipidic microdomains, the docking and fusion machinery, and the cytoskeleton also contribute to the dynamics of receptor trafficking at the synapse.

Indexed as

Protein TransportAnimalsCell LineCell PolarityCytoskeletonDogsExocytosisHumansMembrane FusionMembrane MicrodomainsMembrane ProteinsModels, NeurologicalMuscle ProteinsNerve Tissue ProteinsNeuromuscular JunctionProtein Interaction MappingMembrane ProteinsMuscle ProteinsNerve Tissue ProteinsProtein Sorting SignalsReceptors, NeurotransmitterRNA, Messenger

Identifiers

PMID12392061
OpenAlexW2054359645

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.