Evidence map›Paper›PMID 31623073›Full record

ArticleToxins2019

A Taxon-Specific and High-Throughput Method for Measuring Ligand Binding to Nicotinic Acetylcholine Receptors.

Christina N Zdenek, Richard J Harris, Sanjaya Kuruppu, Nicholas J Youngman, James S Dobson, Jordan Debono, Muzaffar Khan, Ian Smith, Mike Yarski, David Harrich and 4 more

Abstract readComparative Study
In one paragraph

Article in Toxins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

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  20. Phylogenetically diverse diets favor more complex venoms in North American pitvipers.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

14 authors.

Christina N ZdenekVenom Evolution Lab, School of Biological Sciences, The University of Queensland, St. Lucia, QLD 4072, Australia. christinazdenek@gmail.com.ORCID 0000-0002-0385-500X
Richard J HarrisVenom Evolution Lab, School of Biological Sciences, The University of Queensland, St. Lucia, QLD 4072, Australia. rharris2727@googlemail.com.ORCID 0000-0002-4412-2275
Sanjaya KuruppuDepartment of Biochemistry & Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. sanjaya.kuruppu@monash.edu.
Nicholas J YoungmanVenom Evolution Lab, School of Biological Sciences, The University of Queensland, St. Lucia, QLD 4072, Australia. n.youngman@uq.edu.au.
James S DobsonVenom Evolution Lab, School of Biological Sciences, The University of Queensland, St. Lucia, QLD 4072, Australia. j.dobson@uq.edu.au.ORCID 0000-0002-4422-0975
Jordan DebonoVenom Evolution Lab, School of Biological Sciences, The University of Queensland, St. Lucia, QLD 4072, Australia. jordan_debono@hotmail.com.
Muzaffar KhanInstitute of Biology, Leiden University (IBL), Sylvius Laboratory, Sylviusweg 72, 2333 BE Leiden, The Netherlands. m.a.khan@biology.leidenuniv.nl.
Ian SmithDepartment of Biochemistry & Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. ian.smith@monash.edu.
Mike YarskiMillennium Science, 4 Miles Street Mulgrave, VIC 3170, Australia. myarski@mscience.com.au.
David HarrichQIMR Berghofer, Royal Brisbane Hospital QLD 4029, Australia. David.Harrich@qimrberghofer.edu.au.
Charlotte SweeneyTranslational Research Institute, University of Queensland, QLD 4072, Australia. csweeney@vaxxas.com.
Nathan DunstanVenom Supplies Pty Ltd., Stonewell Rd, Tanunda, SA 5352, Australia.
Luke AllenVenom Supplies Pty Ltd., Stonewell Rd, Tanunda, SA 5352, Australia.
Bryan G FryVenom Evolution Lab, School of Biological Sciences, The University of Queensland, St. Lucia, QLD 4072, Australia. bgfry@uq.edu.au.ORCID 0000-0001-6661-1283

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The binding of compounds to nicotinic acetylcholine receptors is of great interest in biomedical research. However, progress in this area is hampered by the lack of a high-throughput, cost-effective, and taxonomically flexible platform. Current methods are low-throughput, consume large quantities of sample, or are taxonomically limited in which targets can be tested. We describe a novel assay which utilizes a label-free bio-layer interferometry technology, in combination with adapted mimotope peptides, in order to measure ligand binding to the orthosteric site of nicotinic acetylcholine receptor alpha-subunits of diverse organisms. We validated the method by testing the evolutionary patterns of a generalist feeding species (

Indexed as

Snake VenomsAnimalsBinding SitesBirdsColubridaeElapidaeHigh-Throughput Screening AssaysHumansLigandsLizardsMarsupialiaOphiophagus hannahPeptidesPhylogenyReceptors, NicotinicRodentiaLigandsPeptidesReceptors, NicotinicSnake Venomsbiosensorevolutionligandnicotinic acetylcholine receptorvenom

Identifiers

PMID31623073
PMCPMC6832995

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.