Evidence map›Paper›PMID 28096462›Full record

ArticleThe Journal of biological chemistry2017

Unique Contributions of an Arginine Side Chain to Ligand Recognition in a Glutamate-gated Chloride Channel.

Timothy Lynagh, Vitaly V Komnatnyy, Stephan A Pless

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

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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.

Timothy LynaghFrom the Center for Biopharmaceuticals, Department of Drug Design and Pharmacology, University of Copenhagen, 2100 H Copenhagen, Denmark.
Vitaly V KomnatnyyFrom the Center for Biopharmaceuticals, Department of Drug Design and Pharmacology, University of Copenhagen, 2100 H Copenhagen, Denmark.
Stephan A PlessFrom the Center for Biopharmaceuticals, Department of Drug Design and Pharmacology, University of Copenhagen, 2100 H Copenhagen, Denmark stephan.pless@sund.ku.dk.ORCID 0000-0001-6654-114X
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutamate recognition by neurotransmitter receptors often relies on Arg residues in the binding site, leading to the assumption that charge-charge interactions underlie ligand recognition. However, assessing the precise chemical contribution of Arg side chains to protein function and pharmacology has proven to be exceedingly difficult in such large and complex proteins. Using the

Indexed as

AnimalsArginineBinding SitesCanavanineChloride ChannelsDrosophila melanogasterGlutamic AcidHaemonchusHumansHydrogen BondingHydrogen-Ion ConcentrationLigandsMutagenesisMutationNeurotransmitter AgentsOocytesArginineCanavanineChloride Channelsglutamate-gated chloride channelsGlutamic AcidLigandsNeurotransmitter AgentsSaltsargininebiophysicschannel activationglutamateion channelligand recognitionmembrane proteinneurotransmitterUnnatural amino acids

Identifiers

PMID28096462
PMCPMC5339774
OpenAlexW2572278370

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.