Evidence map›Paper›PMID 40195322›Full record

ArticleCell discovery2025

Structural basis for allosteric agonism of human α7 nicotinic acetylcholine receptors.

Sanling Liu, Yining Zheng, Haopeng Chen, Xin Li, Qipeng Yan, Wenjun Mu, Yaning Fu, Huan Chen, Hongwei Hou, Lei Liu and 1 more

Abstract read
In one paragraph

Article in Cell discovery, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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 · 2026
    Article
  5. Article
  6. Article
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

11 authors.

Sanling Liu *Division of Life Sciences and Medicine, Joint Center for Biological Analytical Chemistry, Anhui Engineering Laboratory of Peptide Drug, University of Science and Technology of China, Hefei, Anhui, China. sanling@ustc.edu.cn.
Yining Zheng *Division of Life Sciences and Medicine, Joint Center for Biological Analytical Chemistry, Anhui Engineering Laboratory of Peptide Drug, University of Science and Technology of China, Hefei, Anhui, China.
Haopeng ChenDivision of Life Sciences and Medicine, Joint Center for Biological Analytical Chemistry, Anhui Engineering Laboratory of Peptide Drug, University of Science and Technology of China, Hefei, Anhui, China.
Xin LiBeijing Life Science Academy, Beijing, China.ORCID http://orcid.org/0009-0009-3025-673X
Qipeng YanDivision of Life Sciences and Medicine, Joint Center for Biological Analytical Chemistry, Anhui Engineering Laboratory of Peptide Drug, University of Science and Technology of China, Hefei, Anhui, China.ORCID http://orcid.org/0009-0002-8582-0210
Wenjun MuBeijing Life Science Academy, Beijing, China.
Yaning FuBeijing Life Science Academy, Beijing, China.
Huan ChenBeijing Life Science Academy, Beijing, China.
Hongwei HouBeijing Life Science Academy, Beijing, China. qsfctc@163.com.
Lei LiuDepartment of Chemistry, Tsinghua University, Beijing, China. lliu@mail.tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-6290-8602
Changlin TianDivision of Life Sciences and Medicine, Joint Center for Biological Analytical Chemistry, Anhui Engineering Laboratory of Peptide Drug, University of Science and Technology of China, Hefei, Anhui, China. cltian@ustc.edu.cn.ORCID http://orcid.org/0000-0001-9315-900X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The α7 nicotinic acetylcholine receptor (nAChR), a pentameric ligand-gated ion channel, plays important roles in cognition, neuroprotection, and anti-inflammation. As a potential drug target, α7 nAChR has different binding sites for different ligands, particularly agonists and positive allosteric modulators (PAMs). Ago-PAMs can both directly activate and allosterically modulate α7 nAChR. However, the mechanism underlying α7 nAChR modulation by ago-PAM has yet to be fully elucidated. Here, we present cryo-EM structures of α7 nAChR in complex with the ago-PAM GAT107 and Ca

Identifiers

PMID40195322
PMCPMC11977206

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.