Evidence map›Paper›PMID 40349453›Full record

ReviewCurrent opinion in neurobiology2025

The diverse roles of complex glycans in synapse development and function.

Hong Lu, Lexia Bao, Peng Zhang

Abstract readReview
In one paragraph

Review in Current opinion in neurobiology, 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. Article
  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

3 authors.

Hong LuUniversity of British Columbia, Vancouver, BC V6T 1Z3, Canada.
Lexia BaoUniversity of British Columbia, Vancouver, BC V6T 1Z3, Canada.
Peng ZhangDepartment of Neurosciences, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. Electronic address: pxz187@case.edu.

Funding

The role of heparan sulfate modification on neurexin1 in synapse developmentR01MH130476 · NIMH · CASE WESTERN RESERVE UNIVERSITY · PI peng zhang · 2024 to 2026
$1.3M
NIMH NIH HHS R01 MH130476
6 · The paper itself

Abstract

Protein glycosylation is a critical post-translational modification that mediates a myriad of biological functions, including neuronal development in the brain. Stages of neuronal development include neurogenesis, neuronal migration, axonal guidance, synapse formation, and activity-dependent synaptic remodeling and plasticity. Among these, synapse formation and plasticity are essential to establish and maintain neuronal circuits for proper brain function. Yet, the physiological role of glycans at synapses remains poorly understood. This is especially true for complex glycans, known for decades to be present on the cell surface or extracellular matrix, including the microenvironment around synapses. In this review, we highlight recent examples of complex glycans to illustrate their roles in synapse formation and function. Based on these advances, we propose three principal models to categorize all examples in our discussion. We hope this will be beneficial for the field to begin a discussion on the conceptual framework underlying the role of glycans at synapses.

Indexed as

BrainNeurogenesisNeuronal PlasticityNeuronsPolysaccharidesSynapsesAnimalsHumansPolysaccharides

Identifiers

PMID40349453
PMCPMC12461610

What OpenQuestion holds

Textmetadata
LicenceTDM
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.