Evidence map›Paper›PMID 32060286›Full record

ArticleNature communications2020

Structure of formylpeptide receptor 2-G

Youwen Zhuang, Heng Liu, X Edward Zhou, Ravi Kumar Verma, Parker W de Waal, Wonjo Jang, Ting-Hai Xu, Lei Wang, Xing Meng, Gongpu Zhao and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Investigation into ligand selectivity and bias at the formyl peptide receptor family.The Journal of pharmacology and experimental therapeutics · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. TheFrontiers in immunology · 2025
    Review
  15. Molecular basis of lipid and ligand regulation of prostaglandin receptor DP2.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024
    Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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

16 authors.

Youwen Zhuang *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Heng Liu *Laboratory for GPCR Biology, Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, University of Pittsburgh, Pittsburgh, PA, 15261, USA.
X Edward ZhouCenter for Cancer and Cell Biology, Program for Structural Biology, Van Andel Research Institute, Grand Rapids, MI, 49503, USA.
Ravi Kumar VermaBioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Parker W de WaalCenter for Cancer and Cell Biology, Program for Structural Biology, Van Andel Research Institute, Grand Rapids, MI, 49503, USA.
Wonjo JangDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, GA, 30912, USA.ORCID http://orcid.org/0000-0002-1928-8978
Ting-Hai XuCenter for Cancer and Cell Biology, Program for Structural Biology, Van Andel Research Institute, Grand Rapids, MI, 49503, USA.ORCID http://orcid.org/0000-0003-2239-1420
Lei WangLaboratory for GPCR Biology, Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, University of Pittsburgh, Pittsburgh, PA, 15261, USA.ORCID http://orcid.org/0000-0002-3024-8627
Xing MengDavid Van Andel Advanced Cryo-Electron Microscopy Suite, Van Andel Research Institute, Grand Rapids, MI, 49503, USA.
Gongpu ZhaoDavid Van Andel Advanced Cryo-Electron Microscopy Suite, Van Andel Research Institute, Grand Rapids, MI, 49503, USA.ORCID http://orcid.org/0000-0003-0330-1581
Yanyong KangCenter for Cancer and Cell Biology, Program for Structural Biology, Van Andel Research Institute, Grand Rapids, MI, 49503, USA.
Karsten MelcherCenter for Cancer and Cell Biology, Program for Structural Biology, Van Andel Research Institute, Grand Rapids, MI, 49503, USA.ORCID http://orcid.org/0000-0002-9125-4027
Hao FanBioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Nevin A LambertDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, GA, 30912, USA.ORCID http://orcid.org/0000-0001-7550-0921
H Eric XuThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China. Eric.Xu@simm.ac.cn.
Cheng ZhangLaboratory for GPCR Biology, Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, University of Pittsburgh, Pittsburgh, PA, 15261, USA. chengzh@pitt.edu.ORCID http://orcid.org/0000-0001-9042-4007

Funding

Structure, pharmacology and signaling of G protein-coupled receptors (GPCRs) in inflammationR35GM128641 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CHENG ZHANG · 2018 to 2026
$3.5M
Direct assessment of GPCR-transducer coupling and G protein subtype biasR01GM130142 · NIGMS · AUGUSTA UNIVERSITY · PI LAMBERT, NEVIN ALAN · 2018 to 2021
$1.5M
Structural and Functional Studies of Rhodopsin and G-Protein Coupled Receptor KinasesR01GM127710 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2018 to 2020
$1.1M
NIGMS NIH HHS R01 GM127710NIGMS NIH HHS R01 GM130142NIGMS NIH HHS R35 GM128641
6 · The paper itself

Abstract

Formylpeptide receptors (FPRs) as G protein-coupled receptors (GPCRs) can recognize formylpeptides derived from pathogens or host cells to function in host defense and cell clearance. In addition, FPRs, especially FPR2, can also recognize other ligands with a large chemical diversity generated at different stages of inflammation to either promote or resolve inflammation in order to maintain a balanced inflammatory response. The mechanism underlying promiscuous ligand recognition and activation of FPRs is not clear. Here we report a cryo-EM structure of FPR2-G

Indexed as

AnimalsBinding SitesCryoelectron MicroscopyHumansLigandsMolecular Docking SimulationMutationPeptidesProtein ConformationRatsReceptors, Formyl PeptideReceptors, LipoxinSignal TransductionFPR2 protein, humanLigandsPeptidesReceptors, Formyl PeptideReceptors, Lipoxin

Identifiers

PMID32060286
PMCPMC7021761

What Socratic 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 Socratic graph.