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http://purl.uniprot.org/citations/16621800http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16621800http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16621800http://www.w3.org/2000/01/rdf-schema#comment"The SNARE proteins are essential components of the intracellular fusion machinery. It is thought that they form a tight four-helix complex between membranes, in effect initiating fusion. Most SNAREs contain a single coiled-coil region, referred to as the SNARE motif, directly adjacent to a single transmembrane domain. The neuronal SNARE SNAP-25 defines a subfamily of SNARE proteins with two SNARE helices connected by a longer linker, comprising also the proteins SNAP-23 and SNAP-29. We now report the initial characterization of a novel vertebrate homologue termed SNAP-47. Northern blot and immunoblot analysis revealed ubiquitous tissue distribution, with particularly high levels in nervous tissue. In neurons, SNAP-47 shows a widespread distribution on intracellular membranes and is also enriched in synaptic vesicle fractions. In vitro, SNAP-47 substituted for SNAP-25 in SNARE complex formation with the neuronal SNAREs syntaxin 1a and synaptobrevin 2, and it also substituted for SNAP-25 in proteoliposome fusion. However, neither complex assembly nor fusion was as efficient as with SNAP-25."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m513838200"xsd:string
http://purl.uniprot.org/citations/16621800http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m513838200"xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Holt M."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Holt M."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Jahn R."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Jahn R."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Takamori S."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Takamori S."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Varoqueaux F."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Varoqueaux F."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Fasshauer D."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Fasshauer D."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Wiederhold K."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/author"Wiederhold K."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/pages"17076-17083"xsd:string
http://purl.uniprot.org/citations/16621800http://purl.uniprot.org/core/pages"17076-17083"xsd:string