| http://purl.uniprot.org/citations/15876431 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15876431 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15876431 | http://www.w3.org/2000/01/rdf-schema#comment | "SNAREs (soluble N-ethyl-maleimide sensitive factor attachment protein receptors) which locate on the specific organelle membrane assure the correct vesicular transport by mediating specific membrane fusions. SNAREs are referred to as R- or Q-SNAREs on the basis of the amino acid sequence similarities and specific conserved residues. All of the Arabidopsis R-SNAREs have a N-terminal domain, called the longin domain (LD). In this study, we investigated the vacuolar targeting mechanism of Arabidopsis R-SNAREs. The vacuolar localized AtVAMP711 was used as the mother protein of GFP-tagged chimeric proteins joined to several domains such as the LD, the SNARE motif (SNM) and the transmembrane domain (TMD) of other organelle-localized R-SNAREs. The results showed that, whereas the TMD is not relevant for the vacuolar targeting, a complete LD is essential for the vacuolar and subcellular targeting."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2005.04.022"xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2005.04.022"xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/author | "Uemura T."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/author | "Uemura T."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/author | "Takeyasu K."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/author | "Takeyasu K."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/author | "Sato M.H."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/author | "Sato M.H."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/name | "FEBS Lett."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/name | "FEBS Lett."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/pages | "2842-2846"xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/pages | "2842-2846"xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/title | "The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/title | "The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana."xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/volume | "579"xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://purl.uniprot.org/core/volume | "579"xsd:string |
| http://purl.uniprot.org/citations/15876431 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15876431 |
| http://purl.uniprot.org/citations/15876431 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15876431 |
| http://purl.uniprot.org/citations/15876431 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15876431 |
| http://purl.uniprot.org/citations/15876431 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15876431 |