http://purl.uniprot.org/citations/16621800 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16621800 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16621800 | http://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/16621800 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m513838200"xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m513838200"xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Holt M."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Holt M."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Jahn R."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Jahn R."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Urlaub H."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Urlaub H."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Takamori S."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Takamori S."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Varoqueaux F."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Varoqueaux F."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Fasshauer D."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Fasshauer D."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Wiederhold K."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/author | "Wiederhold K."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/pages | "17076-17083"xsd:string |
http://purl.uniprot.org/citations/16621800 | http://purl.uniprot.org/core/pages | "17076-17083"xsd:string |