Literature DB >> 2473923

Charybdotoxin blocks dendrotoxin-sensitive voltage-activated K+ channels.

H Schweitz1, C E Stansfeld, J N Bidard, L Fagni, P Maes, M Lazdunski.   

Abstract

Charybdotoxin, a short scorpion venom neurotoxin, which was thought to be specific for the blockade of Ca2+-activated K+ channels also blocks a class of voltage-sensitive K+ channels that are known to be the target of other peptide neurotoxins from snake and bee venoms such as dendrotoxin and MCD peptide. Charybdotoxin also inhibits 125I-dendrotoxin and 125I-MCD peptide binding to their receptors. All these effects are observed with an IC50 of about 30 nM.

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Year:  1989        PMID： 2473923     DOI： 10.1016/0014-5793(89)80788-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  15 in total

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10.  Tityustoxin K alpha blocks voltage-gated noninactivating K+ channels and unblocks inactivating K+ channels blocked by alpha-dendrotoxin in synaptosomes.

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