Evidence map›Paper›PMID 33232657›Full record

ArticleMolecular cell2021

Structural Basis for High-Affinity Trapping of the Na

Goragot Wisedchaisri, Lige Tonggu, Tamer M Gamal El-Din, Eedann McCord, Ning Zheng, William A Catterall

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 78 citations in OpenAlex.

  1. Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026
    Review
  2. Electrostatic tuning of NaThe Journal of physiology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Refining the NaFEBS letters · 2025
    Article
  12. Structural basis of inhibition of human NaNature communications · 2025
    Article
  13. Review
  14. A structural atlas of druggable sites on NaChannels (Austin, Tex.) · 2024
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Structural basis of inhibition of human NabioRxiv : the preprint server for biology · 2024
    Article
  20. 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

6 authors at 2 institutions in 1 country.

Goragot WisedchaisriDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Lige TongguDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Tamer M Gamal El-DinDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Eedann McCordDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Ning ZhengDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA. Electronic address: nzheng@uw.edu.
William A CatterallDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA. Electronic address: wcatt@uw.edu.
University of Washington · USHoward Hughes Medical Institute · US

Funding

Pharmacological Sciences SupplementT32GM007750 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 1985 to 2023
$12.6M
Structural Basis for Antiarrhythmic Drug ActionR01HL112808 · NHLBI · UNIVERSITY OF WASHINGTON · PI ZHENG, NING · 2012 to 2025
$7.8M
Sodium and Calcium Channels: Structure, Function, Neuroplasticity, and DiseaseR35NS111573 · NINDS · UNIVERSITY OF WASHINGTON · PI SCOTT, JOHN D · 2019 to 2024
$6.1M
VOLTAGE-SENSITIVE SODIUM CHANNELS IN BRAINR01NS015751 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 1985 to 2018
$6.0M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL112808NIGMS NIH HHS T32 GM007750NINDS NIH HHS R01 NS015751NINDS NIH HHS R35 NS111573
6 · The paper itself

Abstract

Voltage-gated sodium channels initiate electrical signals and are frequently targeted by deadly gating-modifier neurotoxins, including tarantula toxins, which trap the voltage sensor in its resting state. The structural basis for tarantula-toxin action remains elusive because of the difficulty of capturing the functionally relevant form of the toxin-channel complex. Here, we engineered the model sodium channel Na

Indexed as

Amino Acid SubstitutionAnimalsHumansMutation, MissenseNAV1.7 Voltage-Gated Sodium ChannelSf9 CellsSpider VenomsSpodopteraNAV1.7 Voltage-Gated Sodium ChannelSCN9A protein, humanSpider Venomsanalgesicscryo-EMelectrophysiologygating-modifier toxinshuwentoxinNaV1.7painprotein structuretarantulavoltage-gated sodium channel

Identifiers

PMID33232657
PMCPMC8043720
OpenAlexW3108747742

What OpenQuestion holds

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LicenceTDM
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.