Evidence map›Paper›PMID 38346960›Full record

ArticleCell discovery2024

Molecular features of the ligand-free GLP-1R, GCGR and GIPR in complex with G

Zhaotong Cong, Fenghui Zhao, Yang Li, Gan Luo, Yiting Mai, Xianyue Chen, Yanyan Chen, Shi Lin, Xiaoqing Cai, Qingtong Zhou and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cell discovery, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
5.4field-weighted citation impact, top 3% of its field
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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. A novel brachydactyly type E syndrome caused by variants in helix 8 of the PTH1R.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2026
    Article
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  6. Review
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  14. Glucagon-like peptide-1 receptor: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2024 · on this map
    Review
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 at 5 institutions in 2 countries.

Zhaotong Cong *Department of Pharmacology, School of Basic Medical Sciences, Fudan University, Shanghai, China.
Fenghui Zhao *State Key Laboratory of Chemical Biology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Yang LiShanghai Institute of Infectious Disease and Biosecurity, Department of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai, China.
Gan LuoKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China.
Yiting MaiResearch Center for Deepsea Bioresources, Sanya, Hainan, China.
Xianyue ChenResearch Center for Deepsea Bioresources, Sanya, Hainan, China.
Yanyan ChenResearch Center for Deepsea Bioresources, Sanya, Hainan, China.
Shi LinResearch Center for Deepsea Bioresources, Sanya, Hainan, China.
Xiaoqing CaiState Key Laboratory of Chemical Biology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Qingtong ZhouDepartment of Pharmacology, School of Basic Medical Sciences, Fudan University, Shanghai, China. zhouqt@fudan.edu.cn.ORCID http://orcid.org/0000-0001-8124-3079
Dehua YangState Key Laboratory of Chemical Biology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China. dhyang@simm.ac.cn.ORCID http://orcid.org/0000-0003-3028-3243
Ming-Wei WangResearch Center for Deepsea Bioresources, Sanya, Hainan, China. mwwang@simm.ac.cn.ORCID http://orcid.org/0000-0001-6550-9017
Institute of Deep-Sea Science and Engineering · CNChinese Academy of Sciences · CNFudan University · CNShanghai Medical College of Fudan University · CNShanghai Institute of Materia Medica · CN

Funding

China Postdoctoral Science Foundation 2022M710806China Postdoctoral Science Foundation 2022M713266National Natural Science Foundation of China (National Science Foundation of China) 32200576National Natural Science Foundation of China (National Science Foundation of China) 81872915; 82073904; 82273961National Natural Science Foundation of China (National Science Foundation of China) 82204474National Natural Science Foundation of China (National Science Foundation of China) 82273985; 82121005; 81973373
6 · The paper itself

Abstract

Class B1 G protein-coupled receptors (GPCRs) are important regulators of many physiological functions such as glucose homeostasis, which is mainly mediated by three peptide hormones, i.e., glucagon-like peptide-1 (GLP-1), glucagon (GCG), and glucose-dependent insulinotropic polypeptide (GIP). They trigger a cascade of signaling events leading to the formation of an active agonist-receptor-G protein complex. However, intracellular signal transducers can also activate the receptor independent of extracellular stimuli, suggesting an intrinsic role of G proteins in this process. Here, we report cryo-electron microscopy structures of the human GLP-1 receptor (GLP-1R), GCG receptor (GCGR), and GIP receptor (GIPR) in complex with G

Identifiers

PMID38346960
PMCPMC10861504
OpenAlexW4391784887

What OpenQuestion holds

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Read underepoch 390

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.