Evidence map›Paper›PMID 32218140›Full record

ArticleToxins2020

Aspartic Acid Isomerization Characterized by High Definition Mass Spectrometry Significantly Alters the Bioactivity of a Novel Toxin from

Stephen R Johnson, Hillary G Rikli

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

Article in Toxins, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 6 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

2 authors at 1 institution in 1 country.

Stephen R JohnsonCarbon Dynamics Institute LLC, Sherman, IL 62684, USA.
Hillary G RikliCollege of Liberal Arts & Sciences, University of Illinois Springfield, Springfield, IL 62703, USA.
University of Illinois at Springfield · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Research in toxinology has created a pharmacological paradox. With an estimated 220,000 venomous animals worldwide, the study of peptidyl toxins provides a vast number of effector molecules. However, due to the complexity of the protein-protein interactions, there are fewer than ten venom-derived molecules on the market. Structural characterization and identification of post-translational modifications are essential to develop biological lead structures into pharmaceuticals. Utilizing advancements in mass spectrometry, we have created a high definition approach that fuses conventional high-resolution MS-MS with ion mobility spectrometry (HDMS

Indexed as

Ion Mobility SpectrometryMass SpectrometryAmino Acid SequenceAnimalsAspartic AcidBinding SitesCell LineDrug DiscoveryHumansIsomerismMembrane PotentialsNAV1.7 Voltage-Gated Sodium ChannelNeurotoxinsProtein BindingProtein ConformationProtein Processing, Post-TranslationalAspartic AcidNAV1.7 Voltage-Gated Sodium ChannelNeurotoxinsSpider VenomsVoltage-Gated Sodium Channel Agonistsdeamidationhigh definition mass spectrometryion mobilityisomerizationPoecilotheriapoecilotheriatoxinsupplemental activationvenomVoltage-gated sodium channel

Identifiers

PMID32218140
PMCPMC7232244
OpenAlexW3013891781

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.