Trends in Biochemical Sciences
Talking pointTetanus and botulism neurotoxins: a new group of zinc proteases
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Bacterial and Fungal Intracranial Infections
2018, Volpe's Neurology of the NewbornIn vitro potency determination of botulinum neurotoxin B based on its receptor-binding and proteolytic characteristics
2016, Toxicology in VitroCitation Excerpt :The active protease cleaves proteins involved in the exocytosis of acetylcholine, thus inhibiting the release of this neurotransmitter. For BoNT/B, the specific substrate is synaptobrevin (Montecucco and Schiavo, 1993). The range of applications of BoNTs A and B for pharmaceutical and cosmetic purposes is broad and steadily growing, leading to an increasing market for botulinum neurotoxins.
Expression and biochemical characterization of light chains of Botulinum neurotoxin subtypes F5 and F7
2015, Protein Expression and PurificationControl of Hormone Secretion
2015, Endocrinology: Adult and PediatricUnique substrate recognition mechanism of the botulinum neurotoxin D light chain
2013, Journal of Biological ChemistryCitation Excerpt :BoNT causes human and animal botulism, a flaccid paralysis caused by the blocking of neurotransmitter (usually acetylcholine) release at the neuromuscular junction. Among the seven different serotypes, BoNT/A, BoNT/B, BoNT/E, and BoNT/F are involved in human botulism, whereas BoNT/D is responsible mainly for animal botulism (1–3). BoNTs are zinc-dependent proteases and contain a His-Glu-X-X-His zinc-binding motif of metalloendopeptidases in the central region of their light chains (4).