Evidence map›Paper›PMID 41932888›Full record

ArticleNature communications2026

Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.

Su-Yu Ji, Wei-Wei Wang, Yixin Yang, Ping Xu, Jiangrong Zhang, Xinyue Zhao, Kun Xi, Shao-Kun Zang, Dan-Dan Shen, Chunyou Mao and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. A biased allosteric modulator functions as a molecular glue to induce βbioRxiv : the preprint server for biology · 2025
    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

12 authors.

Su-Yu Ji *Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Wei-Wei Wang *Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Yixin Yang *Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Ping XuInstitute of Cytology and Genetics, School of Basic Medical Sciences, Hengyang Medical School, University of South China, Hengyang, China.
Jiangrong ZhangDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Xinyue ZhaoDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Kun XiDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.ORCID http://orcid.org/0000-0003-1650-0002
Shao-Kun ZangDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Dan-Dan ShenDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Chunyou MaoDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.ORCID http://orcid.org/0000-0001-5349-8592
Qingya ShenDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China. shen_qingya@zju.edu.cn.ORCID http://orcid.org/0000-0001-6602-7116
Yan ZhangDepartment of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China. zhang_yan@zju.edu.cn.ORCID http://orcid.org/0000-0003-2189-0244

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32141004National Natural Science Foundation of China (National Science Foundation of China) 81922071National Natural Science Foundation of China (National Science Foundation of China) 92353303
6 · The paper itself

Abstract

G-protein-coupled receptors (GPCRs) are significant signal transducers that exist as monomers and in multiple oligomeric forms. However, molecular mechanism driving their dynamic interconversion to regulate intricate signaling in class A GPCRs remains elusive, compounding our understanding of their related pathophysiological functions. Here, we present a set of 12 assemblies of the apelin receptor (APLNR), including dimeric apo state, agonistic small molecule- or nanobody-bound state of monomeric and dimeric APLNR with and without G-proteins, providing a detailed dynamic view of the monomer-dimer transition. High-resolution cryo-EM structures reveal that different ligands induce varying degrees of pre-dissociation of dimers in the absence of G-protein, with G-protein coupling facilitating the transition from dimeric to monomeric receptor. These insights enhance our understanding of the dynamic regulation of class A GPCRs between monomeric and dimeric forms and advance the rational drug design strategies aimed at selectively modulating of APLNR signaling.

Indexed as

Apelin ReceptorsProtein MultimerizationAnimalsCryoelectron MicroscopyGTP-Binding ProteinsHumansLigandsModels, MolecularProtein BindingSignal TransductionApelin ReceptorsAPLNR protein, humanGTP-Binding ProteinsLigands

Identifiers

PMID41932888
PMCPMC13223242

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Registered trials

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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.