Evidence map›Paper›PMID 35241677›Full record

ArticleNature communications2022

Structural basis of leukotriene B4 receptor 1 activation.

Na Wang, Xinheng He, Jing Zhao, Hualiang Jiang, Xi Cheng, Yu Xia, H Eric Xu, Yuanzheng He

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  9. Article
  10. Structural basis of the cysteinyl leukotriene receptor type 2 activation by LTD4.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Identification ofMolecules (Basel, Switzerland) · 2025
    Article
  12. Molecular mechanism of ligand recognition and activation of lysophosphatidic acid receptor LPAR6.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. 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
  14. Neutrophil diversity and function in health and disease.Signal transduction and targeted therapy · 2024
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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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

8 authors at 3 institutions in 1 country.

Na WangLaboratory of Receptor Structure and Signaling, The HIT Center for Life Sciences, Harbin Institute of Technology, Harbin, 150001, China.
Xinheng HeThe CAS Key Laboratory of Receptor Research and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0001-7813-5480
Jing ZhaoMOE Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology, Department of Chemistry, Tsinghua University, Beijing, 100084, China.
Hualiang JiangThe CAS Key Laboratory of Receptor Research and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0003-0656-6315
Xi ChengThe CAS Key Laboratory of Receptor Research and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0003-3735-645X
Yu XiaMOE Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology, Department of Chemistry, Tsinghua University, Beijing, 100084, China.
H Eric XuThe CAS Key Laboratory of Receptor Research and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-6829-8144
Yuanzheng HeLaboratory of Receptor Structure and Signaling, The HIT Center for Life Sciences, Harbin Institute of Technology, Harbin, 150001, China. ajian.he@hit.edu.cn.ORCID http://orcid.org/0000-0001-9131-140X
Chinese Academy of Sciences · CNHarbin Institute of Technology · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leukotriene B4 receptor 1 (BLT1) plays crucial roles in the acute inflammatory responses and is a valuable target for anti-inflammation treatment, however, the mechanism by which leukotriene B4 (LTB4) activates receptor remains unclear. Here, we report the cryo-electron microscopy (cryo-EM) structure of the LTB4 -bound human BLT1 in complex with a G

Indexed as

Leukotriene B4Receptors, Leukotriene B4Cryoelectron MicroscopyGTP-Binding ProteinsHumansInflammationSignal TransductionStructure-Activity RelationshipGTP-Binding ProteinsLeukotriene B4LTB4R protein, humanReceptors, Leukotriene B4

Identifiers

PMID35241677
PMCPMC8894450
OpenAlexW4220736618

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.