Evidence map›Paper›PMID 36823105›Full record

ArticleNature communications2023

Structural basis of lysophosphatidylserine receptor GPR174 ligand recognition and activation.

Jiale Liang, Asuka Inoue, Tatsuya Ikuta, Ruixue Xia, Na Wang, Kouki Kawakami, Zhenmei Xu, Yu Qian, Xinyan Zhu, Anqi Zhang and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. 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
  10. Review
  11. Article
  12. Article
  13. Article
  14. Constitutive activation mechanism of a class C GPCR.Nature structural & molecular biology · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Cryo-EM structures of human GPR34 enable the identification of selective antagonists.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. 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

13 authors at 2 institutions in 2 countries.

Jiale Liang *Laboratory of Receptor Structure and Signaling, HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, 150001, Harbin, China.
Asuka Inoue *Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai, 980-8578, Miyagi, Japan. iaska@tohoku.ac.jp.ORCID 0000-0003-0805-4049
Tatsuya IkutaGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai, 980-8578, Miyagi, Japan.ORCID 0000-0002-8597-0609
Ruixue XiaLaboratory of Receptor Structure and Signaling, HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, 150001, Harbin, China.
Na WangLaboratory of Receptor Structure and Signaling, HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, 150001, Harbin, China.
Kouki KawakamiGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai, 980-8578, Miyagi, Japan.ORCID 0000-0002-2507-8619
Zhenmei XuLaboratory of Receptor Structure and Signaling, HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, 150001, Harbin, China.
Yu QianLaboratory of Receptor Structure and Signaling, HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, 150001, Harbin, China.
Xinyan ZhuLaboratory of Receptor Structure and Signaling, HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, 150001, Harbin, China.
Anqi ZhangHIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, Harbin, China.
Changyou GuoHIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, Harbin, China.
Zhiwei HuangHIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, Harbin, China.ORCID 0000-0002-8201-9391
Yuanzheng HeLaboratory of Receptor Structure and Signaling, HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology, 150001, Harbin, China. ajian.he@hit.edu.cn.ORCID 0000-0001-9131-140X
Harbin Institute of Technology · CNTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysophosphatidylserine (LysoPS) is a lipid mediator that induces multiple cellular responses through binding to GPR174. Here, we present the cryo-electron microscopy (cryo-EM) structure of LysoPS-bound human GPR174 in complex with G

Indexed as

Receptors, G-Protein-CoupledSignal TransductionCryoelectron MicroscopyHumansLigandsLysophospholipidsGPR174 protein, humanLigandslysophosphatidylserineLysophospholipidsReceptors, G-Protein-Coupled

Identifiers

PMID36823105
PMCPMC9950150
OpenAlexW4321599938

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.