Evidence map›Paper›PMID 17698594›Full record

ArticleThe Journal of general physiology2007

beta-Scorpion toxin modifies gating transitions in all four voltage sensors of the sodium channel.

Fabiana V Campos, Baron Chanda, Paulo S L Beirão, Francisco Bezanilla

Abstract read
In one paragraph

Article in The Journal of general physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Preorganized Electric Fields in Voltage-Gated Sodium Channels.Chembiochem : a European journal of chemical biology · 2025
    Article
  2. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
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  10. Review
  11. Mechanisms of noncovalent β subunit regulation of NaThe Journal of general physiology · 2017
    Article
  12. Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Article
  14. Review
  15. Article
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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

4 authors.

Fabiana V CamposInstitute of Molecular Pediatric Sciences and Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Baron Chanda
Paulo S L Beirão
Francisco Bezanilla

Funding

The Electrophysiological Studies of Voltage Gated ChannelsR01GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1985 to 2025
$9.1M
ELECTROPHYSIOLOGICAL STUDIES OF VOLTAGE GATED CHANNELSR37GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1999 to 2008
$3.7M
NIGMS NIH HHS GM30376NIGMS NIH HHS R01 GM030376NIGMS NIH HHS R37 GM030376
6 · The paper itself

Abstract

Several naturally occurring polypeptide neurotoxins target specific sites on the voltage-gated sodium channels. Of these, the gating modifier toxins alter the behavior of the sodium channels by stabilizing transient intermediate states in the channel gating pathway. Here we have used an integrated approach that combines electrophysiological and spectroscopic measurements to determine the structural rearrangements modified by the beta-scorpion toxin Ts1. Our data indicate that toxin binding to the channel is restricted to a single binding site on domain II voltage sensor. Analysis of Cole-Moore shifts suggests that the number of closed states in the activation sequence prior to channel opening is reduced in the presence of toxin. Measurements of charge-voltage relationships show that a fraction of the gating charge is immobilized in Ts1-modified channels. Interestingly, the charge-voltage relationship also shows an additional component at hyperpolarized potentials. Site-specific fluorescence measurements indicate that in presence of the toxin the voltage sensor of domain II remains trapped in the activated state. Furthermore, the binding of the toxin potentiates the activation of the other three voltage sensors of the sodium channel to more hyperpolarized potentials. These findings reveal how the binding of beta-scorpion toxin modifies channel function and provides insight into early gating transitions of sodium channels.

Indexed as

Allosteric RegulationAnimalsBinding SitesFemaleInsect ProteinsIon Channel GatingKineticsMembrane PotentialsModels, BiologicalMuscle ProteinsMuscle, SkeletalNeurotoxinsOocytesPatch-Clamp TechniquesProtein BindingProtein ConformationInsect ProteinsMuscle ProteinsNeurotoxinsScn4a protein, ratscorpion toxin Ts1, TityusScorpion VenomsSodium Channels

Identifiers

PMID17698594
PMCPMC2151646

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.