Evidence map›Paper›PMID 24413018›Full record

ArticleThe EMBO journal2014

Proteomic screening of glutamatergic mouse brain synaptosomes isolated by fluorescence activated sorting.

Christoph Biesemann, Mads Grønborg, Elisa Luquet, Sven P Wichert, Véronique Bernard, Simon R Bungers, Ben Cooper, Frédérique Varoqueaux, Liyi Li, Jennifer A Byrne and 4 more

Abstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

91 citing papers in PubMed.

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  16. Understanding the molecular diversity of synapses.Nature reviews. Neuroscience · 2025
    Review
  17. Article
  18. Article
  19. Review
  20. Review

31 more citing papers are in PubMed but not listed here.

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

14 authors.

Christoph BiesemannDepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Mads Grønborg
Elisa Luquet
Sven P Wichert
Véronique Bernard
Simon R Bungers
Ben Cooper
Frédérique Varoqueaux
Liyi Li
Jennifer A Byrne
Henning Urlaub
Olaf Jahn
Nils Brose
Etienne Herzog

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For decades, neuroscientists have used enriched preparations of synaptic particles called synaptosomes to study synapse function. However, the interpretation of corresponding data is problematic as synaptosome preparations contain multiple types of synapses and non-synaptic neuronal and glial contaminants. We established a novel Fluorescence Activated Synaptosome Sorting (FASS) method that substantially improves conventional synaptosome enrichment protocols and enables high-resolution biochemical analyses of specific synapse subpopulations. Employing knock-in mice with fluorescent glutamatergic synapses, we show that FASS isolates intact ultrapure synaptosomes composed of a resealed presynaptic terminal and a postsynaptic density as assessed by light and electron microscopy. FASS synaptosomes contain bona fide glutamatergic synapse proteins but are almost devoid of other synapse types and extrasynaptic or glial contaminants. We identified 163 enriched proteins in FASS samples, of which FXYD6 and Tpd52 were validated as new synaptic proteins. FASS purification thus enables high-resolution biochemical analyses of specific synapse subpopulations in health and disease.

Indexed as

AnimalsBrainCell SeparationFlow CytometryGlutamic AcidIon ChannelsMiceMice, KnockoutNeuronsProteomicsSynapsesSynaptosomesVesicular Glutamate Transport Protein 1FXYD6 protein, mouseGlutamic AcidIon ChannelsSlc17a7 protein, mouseVesicular Glutamate Transport Protein 1

Identifiers

PMID24413018
PMCPMC3989609

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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.