Unknown

Dataset Information

0

The zinc-dependent protease activity of the botulinum neurotoxins.


ABSTRACT: The botulinum neurotoxins (BoNT, serotypes A-G) are some of the most toxic proteins known and are the causative agents of botulism. Following exposure, the neurotoxin binds and enters peripheral cholinergic nerve endings and specifically and selectively cleaves one or more SNARE proteins to produce flaccid paralysis. This review centers on the kinetics of the Zn-dependent proteolytic activities of these neurotoxins, and briefly describes inhibitors, activators and factors underlying persistence of toxin action. Some of the structural, enzymatic and inhibitor data that are discussed here are available at the botulinum neurotoxin resource, BotDB (http://botdb.abcc.ncifcrf.gov).

SUBMITTER: Lebeda FJ 

PROVIDER: S-EPMC3153231 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

The zinc-dependent protease activity of the botulinum neurotoxins.

Lebeda Frank J FJ   Cer Regina Z RZ   Mudunuri Uma U   Stephens Robert R   Singh Bal Ram BR   Adler Michael M  

Toxins 20100507 5


The botulinum neurotoxins (BoNT, serotypes A-G) are some of the most toxic proteins known and are the causative agents of botulism. Following exposure, the neurotoxin binds and enters peripheral cholinergic nerve endings and specifically and selectively cleaves one or more SNARE proteins to produce flaccid paralysis. This review centers on the kinetics of the Zn-dependent proteolytic activities of these neurotoxins, and briefly describes inhibitors, activators and factors underlying persistence  ...[more]

Similar Datasets

| S-EPMC5923309 | biostudies-literature
| S-EPMC406437 | biostudies-literature
| S-EPMC5394922 | biostudies-literature
| S-EPMC8769338 | biostudies-literature
| S-EPMC1276967 | biostudies-literature
| S-EPMC6070880 | biostudies-literature
| S-EPMC5983264 | biostudies-literature
| S-EPMC5983246 | biostudies-literature
| S-EPMC2730980 | biostudies-literature
| S-EPMC7915854 | biostudies-literature