Evidence map›Paper›PMID 16177043›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005

Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies.

Shuk Yin M Yeung, Dawn Thompson, Zhuren Wang, David Fedida, Brian Robertson

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 20% 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, 1 synthesis or guideline pooled it, 94 citations in OpenAlex.

  1. KFrontiers in pharmacology · 2026
    Pooled it
  2. Review
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  8. Voltage-Gated KMarine drugs · 2024
    Review
  9. Regulation of Neurotransmitter Release by KAdvances in neurobiology · 2023
    Article
  10. Article
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  13. Article
  14. Pharmacology of A-Type KHandbook of experimental pharmacology · 2021
    Article
  15. Peptide Toxins Targeting KV Channels.Handbook of experimental pharmacology · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 2 institutions in 2 countries.

Shuk Yin M YeungNeuroscience Group, School of Biomedical Sciences, University of Leeds, Leeds LS2 9NQ, United Kingdom.
Dawn Thompson
Zhuren Wang
David Fedida
Brian Robertson
University of British Columbia · CAUniversity of Leeds · GB

Funding

Wellcome Trust 060261
6 · The paper itself

Abstract

Kv3 potassium channels, with their ultra-rapid gating and high activation threshold, are essential for high-frequency firing in many CNS neurons. Significantly, the Kv3.4 subunit has been implicated in the major CNS disorders Parkinson's and Alzheimer's diseases, and it is claimed that selectively targeting this subunit will have therapeutic utility. Previous work suggested that BDS toxins ("blood depressing substance," from the sea anemone Anemonia sulcata) were specific blockers for rapidly inactivating Kv3.4 channels, and consequently these toxins are increasingly used as diagnostic agents for Kv3.4 subunits in central neurons. However, precisely how selective are these toxins for this important CNS protein? We show that BDS is not selective for Kv3.4 but markedly inhibits current through Kv3.1 and Kv3.2 channels. Inhibition comes about not by "pore block" but by striking modification of Kv3 gating kinetics and voltage dependence. Activation and inactivation kinetics are slowed by BDS-I and BDS-II, and V(1/2) for activation is shifted to more positive voltages. Alanine substitution mutagenesis around the S3b and S4 segments of Kv3.2 reveals that BDS acts via voltage-sensing domains, and, consistent with this, ON gating currents from nonconducting Kv3.2 are markedly inhibited. The altered kinetics and gating properties, combined with lack of subunit selectivity with Kv3 subunits, seriously affects the usefulness of BDS toxins in CNS studies. Furthermore, our results do not easily fit with the voltage sensor "paddle" structure proposed recently for Kv channels. Our data will be informative for experiments designed to dissect out the roles of Kv3 subunits in CNS function and dysfunction.

Indexed as

Sea AnemonesAnimalsCell LineCentral Nervous SystemCnidarian VenomsElectrophysiologyHumansNeurotoxinsPotassium Channel BlockersRatsShaw Potassium ChannelsBDS-I antiviral protein, Anemonia sulcataBDS II protein, Anemonia sulcataCnidarian VenomsNeurotoxinsPotassium Channel BlockersShaw Potassium Channels

Identifiers

PMID16177043
PMCPMC1314979
OpenAlexW1982109872

What OpenQuestion holds

Textmetadata
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.