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http://purl.uniprot.org/citations/20704566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20704566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20704566http://www.w3.org/2000/01/rdf-schema#comment"The extraordinarily high toxicity of botulinum neurotoxins primarily results from their specific binding and uptake into neurons. At motor neurons, the seven BoNT (botulinum neurotoxin) serotypes A-G inhibit acetylcholine release leading to flaccid paralysis. Uptake of BoNT/A, B, E, F and G requires a dual interaction with gangliosides and the synaptic vesicle proteins synaptotagmin or SV2 (synaptic vesicle glycoprotein 2), whereas little is known about the cell entry mechanisms of the serotypes C and D, which display the lowest amino acid sequence identity compared with the other five serotypes. In the present study we demonstrate that the neurotoxicity of BoNT/D depends on the presence of gangliosides by employing phrenic nerve hemidiaphragm preparations derived from mice expressing the gangliosides GM3, GM2, GM1 and GD1a, or only GM3 [a description of our use of ganglioside nomenclature is given in Svennerholm (1994) Prog. Brain Res. 101, XI-XIV]. High-resolution crystal structures of the 50 kDa cell-binding domain of BoNT/D alone and in complex with sialic acid, as well as biological analyses of single-site BoNT/D mutants identified two carbohydrate-binding sites. One site is located at a position previously identified in BoNT/A, B, E, F and G, but is lacking the conserved SXWY motif. The other site, co-ordinating one molecule of sialic acid, resembles the second ganglioside-binding pocket (the sialic-acid-binding site) of TeNT (tetanus neurotoxin)."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.org/dc/terms/identifier"doi:10.1042/bj20101042"xsd:string
http://purl.uniprot.org/citations/20704566http://purl.org/dc/terms/identifier"doi:10.1042/bj20101042"xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Bigalke H."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Bigalke H."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Binz T."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Binz T."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Lee K."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Lee K."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Jin R."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Jin R."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Mahrhold S."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Mahrhold S."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Pich A."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Pich A."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Rummel A."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Rummel A."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Strotmeier J."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Strotmeier J."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Zhou J."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Zhou J."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Volker A.K."xsd:string
http://purl.uniprot.org/citations/20704566http://purl.uniprot.org/core/author"Volker A.K."xsd:string