Evidence map›Paper›PMID 27626375›Full record

ArticleNature2016

X-ray structures define human P2X(3) receptor gating cycle and antagonist action.

Steven E Mansoor, Wei Lü, Wout Oosterheert, Mrinal Shekhar, Emad Tajkhorshid, Eric Gouaux

Open access · greenAbstract read
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 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
24.9field-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

154 citing papers in PubMed, 256 citations in OpenAlex.

  1. Article
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  9. Review
  10. Endogenous forms of ATP-ATPProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Subtype-specific structural features of the hearing loss-associated human P2X2 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. Review

94 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

6 authors at 3 institutions in 1 country.

Steven E MansoorVollum Institute, Oregon Health &Science University, Portland, Oregon 97239, USA.
Wei LüVollum Institute, Oregon Health &Science University, Portland, Oregon 97239, USA.
Wout OosterheertVollum Institute, Oregon Health &Science University, Portland, Oregon 97239, USA.
Mrinal ShekharDepartment of Biochemistry, Center for Biophysics and Quantitative Biology, and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Emad TajkhorshidDepartment of Biochemistry, Center for Biophysics and Quantitative Biology, and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Eric GouauxVollum Institute, Oregon Health &Science University, Portland, Oregon 97239, USA.
Oregon Health & Science University · USUniversity of Illinois Urbana-Champaign · USVollum Institute · US

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI PEROZO, EDUARDO A · 2010 to 2017
$31.9M
WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SCHULTEN, KLAUS · 2012 to 2021
$19.0M
Structural biology of neurotransmitter ion channelsR01GM100400 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI GOUAUX, JAMES E · 2012 to 2020
$2.3M
Structure Function Studies on the Mechanisms of P2X3 Receptor DesensitizationF32GM108391 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MANSOOR, STEVEN ELIAS · 2013 to 2014
$117k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM108391NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM100400NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems. Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors. The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear. Here we report X-ray crystal structures of the human P2X

Indexed as

ApoproteinsBinding, CompetitiveBinding SitesCrystallizationCrystallography, X-RayHumansIon Channel GatingIon TransportLigandsModels, MolecularPorosityProtein ConformationPurinergic AgonistsPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2X3ApoproteinsLigandsPurinergic AgonistsPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2X3

Identifiers

PMID27626375
PMCPMC5161641
OpenAlexW2519597790

What OpenQuestion holds

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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.