Evidence map›Paper›PMID 35676276›Full record

ArticleNature communications2022

Ligand recognition and biased agonism of the D1 dopamine receptor.

Xiao Teng, Sijia Chen, Yingying Nie, Peng Xiao, Xiao Yu, Zhenhua Shao, Sanduo Zheng

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.8field-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

26 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. The structure of the dopamine DScience advances · 2026
    Article
  3. Review
  4. Elucidating biased signaling in class A GPCRs.Trends in pharmacological sciences · 2025
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Estimation of Dopamine DACS chemical neuroscience · 2025
    Article
  11. Article
  12. Characterization of GαiScience · 2025
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Dopamine receptor divergence revealed using a common ligand.Trends in pharmacological sciences · 2023
    Article
  19. Article
  20. 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

7 authors at 4 institutions in 1 country.

Xiao TengTsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, China.ORCID 0000-0002-5975-6254
Sijia ChenNational Institute of Biological Sciences, Beijing, China.
Yingying NieNational Institute of Biological Sciences, Beijing, China.
Peng XiaoKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, Shandong, China.ORCID 0000-0002-9809-3481
Xiao YuKey Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, Shandong, China.ORCID 0000-0003-1119-8334
Zhenhua ShaoDivision of Nephrology and Kidney Research Institute, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu, Sichuan, China.ORCID 0000-0001-7204-801X
Sanduo ZhengTsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, China. zhengsanduo@nibs.ac.cn.ORCID 0000-0002-7784-0177
Chinese Academy of Medical Sciences & Peking Union Medical College · CNNational Institute of Biological Sciences, Beijing · CNShandong University · CNSichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dopamine receptors are widely distributed in the central nervous system and are important therapeutic targets for treatment of various psychiatric and neurological diseases. Here, we report three cryo-electron microscopy structures of the D1 dopamine receptor (D1R)-Gs complex bound to two agonists, fenoldopam and tavapadon, and a positive allosteric modulator LY3154207. The structure reveals unusual binding of two fenoldopam molecules, one to the orthosteric binding pocket (OBP) and the other to the extended binding pocket (EBP). In contrast, one elongated tavapadon molecule binds to D1R, extending from OBP to EBP. Moreover, LY3154207 stabilizes the second intracellular loop of D1R in an alpha helical conformation to efficiently engage the G protein. Through a combination of biochemical, biophysical and cellular assays, we further show that the broad conformation stabilized by two fenoldopam molecules and interaction between TM5 and the agonist are important for biased signaling of D1R.

Indexed as

DopamineFenoldopamCryoelectron MicroscopyDopamine AgonistsLigandsReceptors, Dopamine D1DopamineDopamine AgonistsFenoldopamLigandsReceptors, Dopamine D1

Identifiers

PMID35676276
PMCPMC9177848
OpenAlexW4281667988

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.