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http://purl.uniprot.org/citations/9886085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9886085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9886085http://www.w3.org/2000/01/rdf-schema#comment"Tetanus toxin and the seven serologically distinct botulinal neurotoxins (BoNT/A to BoNT/G) abrogate synaptic transmission at nerve endings through the action of their light chains (L chains), which proteolytically cleave VAMP (vesicle-associated membrane protein)/synaptobrevin, SNAP-25 (synaptosome-associated protein of 25 kDa), or syntaxin. BoNT/C was reported to proteolyze both syntaxin and SNAP-25. Here, we demonstrate that cleavage of SNAP-25 occurs between Arg198 and Ala199, depends on the presence of regions Asn93 to Glu145 and Ile156 to Met202, and requires about 1,000-fold higher L chain concentrations in comparison with BoNT/A and BoNT/E. Analyses of the BoNT/A and BoNT/E cleavage sites revealed that changes in the carboxyl-terminal residues, in contrast with changes in the amino-terminal residues, drastically impair proteolysis. A proteolytically inactive BoNT/A L chain mutant failed to bind to VAMP/synaptobrevin and syntaxin, but formed a stable complex (KD = 1.9 x 10(-7) M) with SNAP-25. The minimal essential domain of SNAP-25 required for cleavage by BoNT/A involves the segment Met146-Gln197, and binding was optimal only with full-length SNAP-25. Proteolysis by BoNT/E required the presence of the domain Ile156-Asp186. Murine SNAP-23 was cleaved by BoNT/E and, to a reduced extent, by BoNT/A, whereas human SNAP-23 was resistant to all clostridial L chains. Lys185Asp or Pro182Arg mutations of human SNAP-23 induced susceptibility toward BoNT/E or toward both BoNT/A and BoNT/E, respectively."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.org/dc/terms/identifier"doi:10.1046/j.1471-4159.1999.0720327.x"xsd:string
http://purl.uniprot.org/citations/9886085http://purl.org/dc/terms/identifier"doi:10.1046/j.1471-4159.1999.0720327.x"xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Bade S."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Bade S."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Binz T."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Binz T."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Doerries C."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Doerries C."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Jahnz M."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Jahnz M."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Nauenburg S."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Nauenburg S."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Niemann H."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Niemann H."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Vaidyanathan V.V."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Vaidyanathan V.V."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Yoshino K."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/author"Yoshino K."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/9886085http://purl.uniprot.org/core/name"J. Neurochem."xsd:string