Evidence map›Paper›PMID 27698419›Full record

ArticleNature2016

X-ray structure of the human α4β2 nicotinic receptor.

Claudio L Morales-Perez, Colleen M Noviello, Ryan E Hibbs

Abstract 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 211 papers.

0numbers the graph read from it
0cells of the map it votes in
211citing papers in PubMed
32.2field-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

211 citing papers in PubMed, 393 citations in OpenAlex.

  1. Article
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  5. Review
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  17. Review
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151 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

3 authors at 1 institution in 1 country.

Claudio L Morales-PerezDepartments of Neuroscience and Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Colleen M NovielloDepartments of Neuroscience and Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Ryan E HibbsDepartments of Neuroscience and Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
The University of Texas Southwestern Medical Center · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structural studies of heteromeric nicotinic acetylcholine receptors - Diversity SupplementR01DA042072 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2016 to 2020
$2.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Structural biology of the alpha4beta2 nicotinic acetylcholine receptorR33DA037492 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2017 to 2018
$802k
3D Structure and Function of Neuronal Nicotinic Acetylcholine ReceptorsR00NS077983 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2012 to 2014
$735k
The Cellular Biophysics of the Neuron Training ProgramT32NS069562 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI KAVALALI, EGE T · 2010 to 2014
$568k
Structural biology of the alpha4beta2 nicotinic acetylcholine receptorR21DA037492 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2014 to 2015
$368k
3D Structure and Function of Neuronal Nicotinic Acetylcholine ReceptorsK99NS077983 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI HIBBS, RYAN E · 2012 to 2012
$92k
NCRR NIH HHS S10 RR029205NIDA NIH HHS R01 DA042072NIDA NIH HHS R21 DA037492NIDA NIH HHS R33 DA037492NIGMS NIH HHS P41 GM103403NINDS NIH HHS K99 NS077983NINDS NIH HHS R00 NS077983NINDS NIH HHS T32 NS069562
6 · The paper itself

Abstract

Nicotinic acetylcholine receptors are ligand-gated ion channels that mediate fast chemical neurotransmission at the neuromuscular junction and have diverse signalling roles in the central nervous system. The nicotinic receptor has been a model system for cell-surface receptors, and specifically for ligand-gated ion channels, for well over a century. In addition to the receptors' prominent roles in the development of the fields of pharmacology and neurobiology, nicotinic receptors are important therapeutic targets for neuromuscular disease, addiction, epilepsy and for neuromuscular blocking agents used during surgery. The overall architecture of the receptor was described in landmark studies of the nicotinic receptor isolated from the electric organ of Torpedo marmorata. Structures of a soluble ligand-binding domain have provided atomic-scale insights into receptor-ligand interactions, while high-resolution structures of other members of the pentameric receptor superfamily provide touchstones for an emerging allosteric gating mechanism. All available high-resolution structures are of homopentameric receptors. However, the vast majority of pentameric receptors (called Cys-loop receptors in eukaryotes) present physiologically are heteromeric. Here we present the X-ray crystallographic structure of the human α4β2 nicotinic receptor, the most abundant nicotinic subtype in the brain. This structure provides insights into the architectural principles governing ligand recognition, heteromer assembly, ion permeation and desensitization in this prototypical receptor class.

Indexed as

Binding SitesBridged Bicyclo Compounds, HeterocyclicCrystallography, X-RayHumansIon TransportLigandsModels, MolecularNeurotransmitter AgentsNicotinic AgonistsProtein Structure, QuaternaryPyridinesReceptors, NicotinicBridged Bicyclo Compounds, HeterocyclicepibatidineLigandsNeurotransmitter AgentsNicotinic Agonistsnicotinic receptor alpha4beta2PyridinesReceptors, Nicotinic

Identifiers

PMID27698419
PMCPMC5161573
OpenAlexW2524130802

What OpenQuestion holds

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LicenceTDM
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.