Charybdotoxin

Known as: ChTX, CTX Toxin, Toxin, Quinquestriatus 
A 37-amino acid residue peptide isolated from the scorpion Leiurus quinquestriatus hebraeus. It is a neurotoxin that inhibits calcium activated… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1985-2017
010203019852017

Papers overview

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Highly Cited
2003
Highly Cited
2003
1. Activation of Ca(2+)-activated K(+)-channels (K(Ca)) has been suggested to play a key role in endothelium-derived… (More)
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2003
2003
I(Ks) voltage-gated K(+) channels contain four pore-forming KCNQ1 subunits and MinK accessory subunits in a number that has been… (More)
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Highly Cited
1999
Highly Cited
1999
In rat mesenteric artery, endothelium-derived hyperpolarizing factor (EDHF) is blocked by a combination of apamin and… (More)
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Highly Cited
1994
Highly Cited
1994
Charybdotoxin (CTX) is a peptide of known structure that inhibits Shaker K+ channels by a pore-blocking mechanism. Point… (More)
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1993
1993
Charybdotoxin block of a Shaker K+ channel was studied in Xenopus oocyte macropatches. Toxin on rate increases linearly with… (More)
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Highly Cited
1992
Highly Cited
1992
Charybdotoxin (ChTX), a K+ channel blocker, depolarizes human peripheral T lymphocytes and renders them insensitive to activation… (More)
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Highly Cited
1989
Highly Cited
1989
The inhibition by charybdotoxin of A-type potassium channels expressed in Xenopus oocytes was studied for several splicing… (More)
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1989
1989
We demonstrate that blockade of the lymphocyte voltage-gated K+ channel by charybdotoxin (CTX) inhibits lymphocyte mitogenesis… (More)
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Highly Cited
1988
Highly Cited
1988
Charybdotoxin (CTX), a small, basic protein from scorpion venom, strongly inhibits the conduction of K ions through high… (More)
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Highly Cited
1985
Highly Cited
1985
The recent development of techniques for recording currents through single ionic channels has led to the identification of a K… (More)
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