Mechanism of action of clostridial neurotoxins and rational inhibitor design

Biology of the Cell

Volumn 92, Issue 6, 2000, Pages 445-447

  Roques, Bernard P ^a   Anne, Christine ^a   Turcaud, Serge ^a   Fournié Zaluski, Marie Claude ^a  

^a INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ALIPHATIC COMPOUND; ANTITOXIN; AROMATIC AMINO ACID; BOTULINUM ANTISERUM; BOTULINUM TOXIN; BOTULINUM TOXIN B; METALLOPROTEINASE; PHENYLALANINE; PROTEIN INHIBITOR; PSEUDOPEPTIDE; SYNAPTOBREVIN; TETANUS TOXIN;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL MODIFICATION; CHEMICAL STRUCTURE; CLOSTRIDIUM BOTULINUM; CLOSTRIDIUM TETANI; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN;

EID: 0033670549     PISSN: 02484900     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0248-4900(00)01098-4     Document Type: Article

References (9)

1. Cooperative exosite-dependent cleavage of synaptobrevin by tetanus toxin light chain
2. Clues to the multi-phasic inhibitory action of botulinum neurotoxins on release of transmitters
3. Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution
4. Metallopeptidase inhibitors of tetanus toxin: A combinatorial approach
5. Bacterial protein toxins penetrate cells via a four-step mechanism
6. Neutral endopeptidase 24.11: Structure, inhibition, and experimental and clinical pharmacology
7. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
8. Clostridium botulinum neurotoxins, their structures and modes of action
9. Peptide substrate specificity and properties of the zinc-endopeptidase activity of botulinum type B neurotoxin