Evidence map›Paper›PMID 40771565›Full record

ReviewFrontiers in cellular neuroscience2025

Proximity labeling uncovers the synaptic proteome under physiological and pathological conditions.

Junpei Matsubayashi, Tetsuya Takano

Abstract readReview
In one paragraph

Review in Frontiers in cellular neuroscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
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.

Junpei MatsubayashiDivision of Molecular Systems for Brain Function, Medical Institute of Bioregulation, Kyushu University Institute for Advanced Study, Fukuoka, Japan.
Tetsuya TakanoDivision of Molecular Systems for Brain Function, Medical Institute of Bioregulation, Kyushu University Institute for Advanced Study, Fukuoka, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synapses are fundamental units of neurotransmission and play a central role in the formation and function of neural circuits. These dynamic structures exhibit morphological and functional plasticity in response to experience and activity, supporting higher brain functions such as learning, memory, and emotion. Their molecular composition includes diverse membrane-associated and cytoskeletal proteins that mediate intercellular signaling, regulate synaptic plasticity, and maintain structural stability. Disruptions in these protein networks, often referred to as synaptopathies, are closely linked to psychiatric and neurological disorders. Such disruptions commonly manifest as region-specific changes in synapse number, morphology, or signaling efficacy. Although a large number of synaptic proteins have been identified through conventional proteomic approaches, our understanding of synaptic specificity and plasticity remains limited. This is primarily due to insufficient spatial resolution, lack of cell-type specificity, and challenges in applying these methods to intact neural circuits

Indexed as

BioIDcytoskeletonproteomicsspine formationsynapsesynaptopathy

Identifiers

PMID40771565
PMCPMC12325354

What OpenQuestion holds

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Registered trials

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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.