ArticleNpj viruses2025
HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors.
Article in Npj viruses, 2025. 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
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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.
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.
- Rabies virus glycoprotein variants modulate neuronal nicotinic receptors in a conformation-dependent manner.Scientific reports · 2026Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herpes virus1(HSV1) is a neurotropic virus that has been linked to Alzheimer's disease. An In-silico structural homology search using α -Bgtx, identified structural homology between HSV1 gD and the nicotinic receptor neurotoxin α-Bgtx. SPR binding studies using acetylcholine binding protein from Lymnaea stagnalis, and functional two electrode voltage clamp studies of α7 nAChRs demonstrate the ability of HSV1 to interact directly with nAChRs. Molecular docking studies support the binding of a neurotoxin-like binding loop in HSV1 to a binding site similar to the neurotoxin binding domain. Interaction of HSV1 with nAChRs provides novel insights into a potential mechanism of action of HSV and its potential role in Alzheimer's disease.
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Registered trials
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