ArticleCommunications biology2026
Branching of O-mannose glycans regulates node of Ranvier organization and saltatory conduction.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
Who cites it
1 citing paper in PubMed.
- Myelin Dynamics at the Axon-Oligodendrocyte Interface: Adaptive Conduction Homeostasis in Demyelination, Remyelination and White Matter Repair.International journal of molecular sciences · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
The myelin sheath of axons is organized into domain structures with nodes of Ranvier that facilitate saltatory conduction. Here, we show that a brain-specific glycosyltransferase, MGAT5B that catalyzes β1,6-GlcNAc branching of an O-mannose (Man) glycan, is required for node of Ranvier integrity. Mgat5b knockout (KO) mice displayed broadening of nodes in brain white matter. Consistently, electrophysiological analysis demonstrated a significant delay and variable axonal conduction in Mgat5b KO mice, indicating the importance of branched O-Man glycans in node morphology and functions. Biochemical and glycoproteomic analyses demonstrated that MGAT5B modifies the glycans of a key node-organizing glycoprotein, neurofascin 186 (NF186), and that interaction between NF186 and Contactin 1 is negatively regulated by branched O-Man glycans. Finally, neuron-specific restoration of MGAT5B in KO mice rescued these nodal defects, indicating a cell-autonomous role of MGAT5B in node organization. Our findings highlight a glycan-mediated mechanism for the maintenance of node structure and function.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.