Evidence map›Paper›PMID 29567943›Full record

ArticleScientific reports2018

Peptide ion channel toxins from the bootlace worm, the longest animal on Earth.

Erik Jacobsson, Håkan S Andersson, Malin Strand, Steve Peigneur, Camilla Eriksson, Henrik Lodén, Mohammadreza Shariatgorji, Per E Andrén, Eline K M Lebbe, K Johan Rosengren and 2 more

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

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

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  17. Compound HeterozygousFrontiers in cardiovascular medicine · 2020
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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

12 authors at 5 institutions in 3 countries.

Erik JacobssonDivision of Pharmacognosy, Department of Medicinal Chemistry, Biomedical Center, Uppsala University, Box 574, SE-751 23, Uppsala, Sweden.
Håkan S AnderssonLinnaeus University Centre for Biomaterials Chemistry, Department of Chemistry and Biomedical Sciences, Linnaeus University, Kalmar, Sweden.
Malin StrandSwedish Species Information Centre, Swedish University of Agricultural Sciences, Uppsala, Sweden.
Steve PeigneurToxicology & Pharmacology, University of Leuven (KU Leuven), O&N 2, PO Box 992, Herestraat 49, 3000, Leuven, Belgium.
Camilla ErikssonDivision of Pharmacognosy, Department of Medicinal Chemistry, Biomedical Center, Uppsala University, Box 574, SE-751 23, Uppsala, Sweden.
Henrik LodénBiomolecular Mass Spectrometry Imaging (BMSI), National and SciLifeLab Resource for Mass Spectrometry Imaging, Department of Pharmaceutical Biosciences, Biomedical Center, Uppsala University, Box 591, SE-751 24, Uppsala, Sweden.
Mohammadreza ShariatgorjiBiomolecular Mass Spectrometry Imaging (BMSI), National and SciLifeLab Resource for Mass Spectrometry Imaging, Department of Pharmaceutical Biosciences, Biomedical Center, Uppsala University, Box 591, SE-751 24, Uppsala, Sweden.
Per E AndrénBiomolecular Mass Spectrometry Imaging (BMSI), National and SciLifeLab Resource for Mass Spectrometry Imaging, Department of Pharmaceutical Biosciences, Biomedical Center, Uppsala University, Box 591, SE-751 24, Uppsala, Sweden.ORCID 0000-0002-4062-7743
Eline K M LebbeToxicology & Pharmacology, University of Leuven (KU Leuven), O&N 2, PO Box 992, Herestraat 49, 3000, Leuven, Belgium.
K Johan RosengrenSchool of Biomedical Sciences, The University of Queensland, Brisbane, QLD 4072, Australia.
Jan TytgatToxicology & Pharmacology, University of Leuven (KU Leuven), O&N 2, PO Box 992, Herestraat 49, 3000, Leuven, Belgium.
Ulf GöranssonDivision of Pharmacognosy, Department of Medicinal Chemistry, Biomedical Center, Uppsala University, Box 574, SE-751 23, Uppsala, Sweden. Ulf.Goransson@fkog.uu.se.ORCID 0000-0002-5005-9612
Uppsala University · SEKU Leuven · BELinnaeus University · SESwedish University of Agricultural Sciences · SEThe University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polypeptides from animal venoms have found important uses as drugs, pharmacological tools, and within biotechnological and agricultural applications. We here report a novel family of cystine knot peptides from nemertean worms, with potent activity on voltage-gated sodium channels. These toxins, named the α-nemertides, were discovered in the epidermal mucus of Lineus longissimus, the 'bootlace worm' known as the longest animal on earth. The most abundant peptide, the 31-residue long α-1, was isolated, synthesized, and its 3D NMR structure determined. Transcriptome analysis including 17 species revealed eight α-nemertides, mainly distributed in the genus Lineus. α-1 caused paralysis and death in green crabs (Carcinus maenas) at 1 µg/kg (~300 pmol/kg). It showed profound effect on invertebrate voltage-gated sodium channels (e.g. Blattella germanica Na

Indexed as

AnimalsBrachyuraChromatography, LiquidCockroachesCystine Knot MotifsDrug DiscoveryExome SequencingHelminthsMucusParalysisPeptidesPhylogenySwedenTandem Mass SpectrometryVenomsVoltage-Gated Sodium ChannelsPeptidesVenomsVoltage-Gated Sodium Channels

Identifiers

PMID29567943
PMCPMC5864730
OpenAlexW2790158123

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.