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• W2021858423 startingPage "6743" @default.
• W2021858423 abstract "The botulinum neurotoxins, characterized by their neuromuscular paralytic effects, are the most toxic proteins known to man. Due to their extreme potency, ease of production, and duration of activity, the BoNT proteins have been classified by the Centers for Disease Control as high threat agents for bioterrorism. In an attempt to discover effective BoNT therapeutics, we have pursued a strategy in which we leverage the blockade of K(+) channels that ultimately results in the reversal of neuromuscular paralysis. Towards this end, we utilized peptides derived from scorpion venom that are highly potent K(+) channel blockers. Herein, we report the synthesis of charybdotoxin, a 37 amino acid peptide, and detail its activity, along with iberiotoxin and margatoxin, in a mouse phrenic nerve hemidiaphragm assay in the absence and the presence of BoNT/A." @default.
• W2021858423 created "2016-06-24" @default.
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• W2021858423 date "2013-12-01" @default.
• W2021858423 modified "2023-10-04" @default.
• W2021858423 title "Scorpion toxins for the reversal of BoNT-induced paralysis" @default.
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• W2021858423 doi "https://doi.org/10.1016/j.bmcl.2013.10.029" @default.
• W2021858423 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3869784" @default.
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