ArticleCellular and molecular life sciences : CMLS2023
Generation of nanobodies acting as silent and positive allosteric modulators of the α7 nicotinic acetylcholine receptor.
Article in Cellular and molecular life sciences : CMLS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Discovery and mechanism of negative allosteric modulation of the α7 nicotinic acetylcholine receptor by nanobodies.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Review
- Targeting ACE2 with a camelid antibody inhibits SARS-CoV-2 binding and has protective effects in vivo.Nature communications · 2025Article
- Structural mechanisms behind the neutralisation of long-chain α-neurotoxins by broadly neutralising VCommunications chemistry · 2025Article
- VHH Nanobody Versatility against Pentameric Ligand-Gated Ion Channels.Journal of medicinal chemistry · 2024Review
- Article
- An original potentiating mechanism revealed by the cryo-EM structures of the human α7 nicotinic receptor in complex with nanobodies.Nature communications · 2023Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 2 countries.
Funding
Abstract
The α7 nicotinic acetylcholine receptor (nAChR), a potential drug target for treating cognitive disorders, mediates communication between neuronal and non-neuronal cells. Although many competitive antagonists, agonists, and partial-agonists have been found and synthesized, they have not led to effective therapeutic treatments. In this context, small molecules acting as positive allosteric modulators binding outside the orthosteric, acetylcholine, site have attracted considerable interest. Two single-domain antibody fragments, C4 and E3, against the extracellular domain of the human α7-nAChR were generated through alpaca immunization with cells expressing a human α7-nAChR/mouse 5-HT
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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.