Evidence map›Paper›PMID 29703751›Full record

ArticleThe Journal of biological chemistry2018

Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes.

Akello J Agwa, Steve Peigneur, Chun Yuen Chow, Nicole Lawrence, David J Craik, Jan Tytgat, Glenn F King, Sónia Troeira Henriques, Christina I Schroeder

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Hyperpolarization Modulation of the T-Type hCaAngewandte Chemie (International ed. in English) · 2025
    Article
  3. Structural basis of inhibition of human NaNature communications · 2025
    Article
  4. Structural basis of inhibition of human NabioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Mapping the Molecular Surface of the Analgesic NaACS pharmacology & translational science · 2020
    Article
  18. Article
  19. Review
  20. 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

9 authors at 2 institutions in 2 countries.

Akello J AgwaFrom the Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia and.ORCID 0000-0001-9295-5071
Steve PeigneurLaboratory of Toxicology and Pharmacology, University of Leuven (KU Leuven), 3000 Leuven, Belgium.
Chun Yuen ChowFrom the Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia and.ORCID 0000-0003-2861-5843
Nicole LawrenceFrom the Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia and.
David J CraikFrom the Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia and.
Jan TytgatLaboratory of Toxicology and Pharmacology, University of Leuven (KU Leuven), 3000 Leuven, Belgium.
Glenn F KingFrom the Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia and.
Sónia Troeira HenriquesFrom the Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia and.
Christina I SchroederFrom the Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia and c.schroeder@imb.uq.edu.au.ORCID 0000-0002-6737-6374
The University of Queensland · AUKU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gating modifier toxins (GMTs) are venom-derived peptides isolated from spiders and other venomous creatures and modulate activity of disease-relevant voltage-gated ion channels and are therefore being pursued as therapeutic leads. The amphipathic surface profile of GMTs has prompted the proposal that some GMTs simultaneously bind to the cell membrane and voltage-gated ion channels in a trimolecular complex. Here, we examined whether there is a relationship among spider GMT amphipathicity, membrane binding, and potency or selectivity for voltage-gated sodium (Na

Indexed as

Amino Acid SequenceAnimalsArthropod ProteinsCell MembraneHEK293 CellsHumansLipid BilayersModels, MolecularNAV1.7 Voltage-Gated Sodium ChannelSpidersSpider VenomsToxins, BiologicalVoltage-Gated Sodium Channel BlockersArthropod ProteinsLipid BilayersNAV1.7 Voltage-Gated Sodium ChannelSpider VenomsToxins, BiologicalVoltage-Gated Sodium Channel Blockersamphipathic surfacedisulfide-rich peptidesgating modifier toxinlipid-protein interactionoxidative foldingpainpeptidespharmacologyrational drug designsodium channeltarantula venomtoxinvoltage sensor domain

Identifiers

PMID29703751
PMCPMC5995520
OpenAlexW2802455578

What OpenQuestion holds

Textmetadata
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.