Evidence map›Paper›PMID 25119048›Full record

ArticleNature2014

X-ray structure of the mouse serotonin 5-HT3 receptor.

Ghérici Hassaine, Cédric Deluz, Luigino Grasso, Romain Wyss, Menno B Tol, Ruud Hovius, Alexandra Graff, Henning Stahlberg, Takashi Tomizaki, Aline Desmyter and 5 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers.

0numbers the graph read from it
0cells of the map it votes in
198citing 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

198 citing papers in PubMed.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Article
  6. RIC-3 Interacts Directly with the 5-HTbioRxiv : the preprint server for biology · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Predicted conformations of 5-HT3 receptor ion channels are modified by subunit D.Computational and structural biotechnology journal · 2025
    Article
  12. Cryo-EM structure of the zinc-activated channel (ZAC) in the Cys-loop receptor superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Progress on functions of intracellular domainZhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024
    Review
  18. Article
  19. Structural basis for partial agonism in 5-HTNature structural & molecular biology · 2024
    Article
  20. Article

138 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

15 authors.

Ghérici Hassaine1] Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland [2] [3] Theranyx, 163 Avenue de Luminy, 13288 Marseille, France.
Cédric Deluz1] Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland [2].
Luigino GrassoLaboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Romain WyssLaboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Menno B TolLaboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Ruud HoviusLaboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Alexandra GraffCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, CH-4058 Basel, Switzerland.
Henning StahlbergCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, CH-4058 Basel, Switzerland.
Takashi TomizakiSwiss Light Source, Paul Scherrer Institute, CH-5234 Villigen, Switzerland.
Aline DesmyterArchitecture et Fonction des Macromolécules Biologiques, CNRS UMR 7257 and Université Aix-Marseille, F-13288 Marseille, France.
Christophe Moreau1] Université Grenoble Alpes, IBS, F-38000 Grenoble, France [2] CNRS, IBS, F-38000 Grenoble, France [3] CEA, DSV, IBS, F-38000 Grenoble, France.
Xiao-Dan LiLaboratory of Biomolecular Research, Paul Scherrer Institute, CH-5232 Villigen, Switzerland.
Frédéric PoitevinUnité de Dynamique Structurale des Macromolécules, Institut Pasteur, CNRS UMR3528, F-75015 Paris, France.
Horst VogelLaboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Hugues Nury1] Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland [2] Université Grenoble Alpes, IBS, F-38000 Grenoble, France [3] CNRS, IBS, F-38000 Grenoble, France [4] CEA, DSV, IBS, F-38000 Grenoble, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurotransmitter-gated ion channels of the Cys-loop receptor family mediate fast neurotransmission throughout the nervous system. The molecular processes of neurotransmitter binding, subsequent opening of the ion channel and ion permeation remain poorly understood. Here we present the X-ray structure of a mammalian Cys-loop receptor, the mouse serotonin 5-HT3 receptor, at 3.5 Å resolution. The structure of the proteolysed receptor, made up of two fragments and comprising part of the intracellular domain, was determined in complex with stabilizing nanobodies. The extracellular domain reveals the detailed anatomy of the neurotransmitter binding site capped by a nanobody. The membrane domain delimits an aqueous pore with a 4.6 Å constriction. In the intracellular domain, a bundle of five intracellular helices creates a closed vestibule where lateral portals are obstructed by loops. This 5-HT3 receptor structure, revealing part of the intracellular domain, expands the structural basis for understanding the operating mechanism of mammalian Cys-loop receptors.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCrystallography, X-RayMiceModels, MolecularMolecular Sequence DataNeurotransmitter AgentsProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsReceptors, Serotonin, 5-HT3Neurotransmitter AgentsProtein SubunitsReceptors, Serotonin, 5-HT3

Identifiers

PMID25119048

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.