Evidence map›Paper›PMID 27595334›Full record

ArticleNature2016

Activation mechanism of endothelin ET

Wataru Shihoya, Tomohiro Nishizawa, Akiko Okuta, Kazutoshi Tani, Naoshi Dohmae, Yoshinori Fujiyoshi, Osamu Nureki, Tomoko Doi

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
  2. The Allosteric Mechanism of G-Protein-Coupled Receptors is Induced Fit, Not Conformational Selection.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Structure of a lasso peptide bound ETNature communications · 2025
    Article
  4. Review
  5. Article
  6. Structure of endothelin ETCommunications biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Insights into Endothelin Receptors in Pulmonary Hypertension.International journal of molecular sciences · 2023
    Review
  18. Article
  19. Article
  20. Article

27 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

8 authors at 5 institutions in 1 country.

Wataru ShihoyaDepartment of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
Tomohiro NishizawaDepartment of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo 113-0032, Japan.
Akiko OkutaCellular and Structural Physiology Institute, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
Kazutoshi TaniCellular and Structural Physiology Institute, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Yoshinori FujiyoshiDepartment of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
Osamu NurekiDepartment of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo 113-0032, Japan.
Tomoko DoiDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Nagoya University · JPJapan Science and Technology Agency · JPKyoto University · JPRIKEN Center for Sustainable Resource Science · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endothelin, a 21-amino-acid peptide, participates in various physiological processes, such as regulation of vascular tone, humoral homeostasis, neural crest cell development and neurotransmission. Endothelin and its G-protein-coupled receptor are involved in the development of various diseases, such as pulmonary arterial hypertension, and thus are important therapeutic targets. Here we report crystal structures of human endothelin type B receptor in the ligand-free form and in complex with the endogenous agonist endothelin-1. The structures and mutation analysis reveal the mechanism for the isopeptide selectivity between endothelin-1 and -3. Transmembrane helices 1, 2, 6 and 7 move and envelop the entire endothelin peptide, in a virtually irreversible manner. The agonist-induced conformational changes are propagated to the receptor core and the cytoplasmic G-protein coupling interface, and probably induce conformational flexibility in TM6. A comparison with the M2 muscarinic receptor suggests a shared mechanism for signal transduction in class A G-protein-coupled receptors.

Indexed as

Allosteric RegulationAllosteric SiteCell MembraneCrystallography, X-RayEndothelin-1Endothelin-3HumansLigandsModels, MolecularProtein ConformationReceptor, Endothelin BReceptor, Muscarinic M2Signal TransductionSubstrate SpecificityEndothelin-1Endothelin-3LigandsReceptor, Endothelin BReceptor, Muscarinic M2

Identifiers

PMID27595334
OpenAlexW2513912936

What OpenQuestion holds

Textmetadata
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.