Evidence map›Paper›PMID 31732432›Full record

ArticleCell chemical biology2020

Development of Photocrosslinking Probes Based on Huwentoxin-IV to Map the Site of Interaction on Nav1.7.

Foteini Tzakoniati, Hui Xu, Tianbo Li, Natalie Garcia, Christine Kugel, Jian Payandeh, Christopher M Koth, Edward W Tate

Abstract read
In one paragraph

Article in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Lysine Targeting Group-Transfer Chimeras for Proximity Induction.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Cystine Knot Peptides with Tuneable Activity and Mechanism.Angewandte Chemie (International ed. in English) · 2022
    Article
  6. Review
  7. Review
  8. Article
  9. Synthetic Analogues of Huwentoxin-IV Spider Peptide With Altered Human NaFrontiers in cell and developmental biology · 2021
    Article
  10. Employing NaChBac for cryo-EM analysis of toxin action on voltage-gated NaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Review
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

8 authors.

Foteini TzakoniatiDepartment of Chemistry, Imperial College London, London W12 0BZ, UK.
Hui XuDepartment of Structural Biology, Genentech, South San Francisco, CA 94080, USA.
Tianbo LiDepartment of Biochemical and Cellular Pharmacology, Genentech, South San Francisco, CA 94080, USA.
Natalie GarciaDepartment of Protein Analytical Chemistry, Genentech, South San Francisco, CA 94080, USA.
Christine KugelDepartment of Biomolecular Resources, Genentech, South San Francisco, CA 94080, USA.
Jian PayandehDepartment of Structural Biology, Genentech, South San Francisco, CA 94080, USA.
Christopher M KothDepartment of Structural Biology, Genentech, South San Francisco, CA 94080, USA.
Edward W TateDepartment of Chemistry, Imperial College London, London W12 0BZ, UK. Electronic address: e.tate@imperial.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/L50239X/1Medical Research Council MC_PC_14128
6 · The paper itself

Abstract

Voltage-gated sodium (Nav) channels respond to changes in the membrane potential of excitable cells through the concerted action of four voltage-sensor domains (VSDs). Subtype Nav1.7 plays an important role in the propagation of signals in pain-sensing neurons and is a target for the clinical development of novel analgesics. Certain inhibitory cystine knot (ICK) peptides produced by venomous animals potently modulate Nav1.7; however, the molecular mechanisms underlying their selective binding and activity remain elusive. This study reports on the design of a library of photoprobes based on the potent spider toxin Huwentoxin-IV and the determination of the toxin binding interface on VSD2 of Nav1.7 through a photocrosslinking and tandem mass spectrometry approach. Our Huwentoxin-IV probes selectively crosslink to extracellular loop S1-S2 and helix S3 of VSD2 in a chimeric channel system. Our results provide a strategy that will enable mapping of sites of interaction of other ICK peptides on Nav channels.

Indexed as

Binding SitesCross-Linking ReagentsHumansModels, MolecularMolecular ProbesNAV1.7 Voltage-Gated Sodium ChannelPhotochemical ProcessesSpider VenomsCross-Linking Reagentshuwentoxin IV, Selenocosmia huwenaMolecular ProbesNAV1.7 Voltage-Gated Sodium ChannelSCN9A protein, humanSpider VenomsdiazirineHuwentoxin-IVinhibitory cystine knotNav1.7peptide mappingphotoaffinity labelingphotocrosslinkingvoltage-gated sodium channel

Identifiers

PMID31732432
PMCPMC7083225

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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.