http://purl.uniprot.org/citations/9657146 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9657146 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9657146 | http://www.w3.org/2000/01/rdf-schema#comment | "Vacuole fusion requires Sec18p (NSF), Sec17p (alpha-SNAP), Ypt7p (GTP binding protein), Vam3p (t-SNARE), Nyv1p (v-SNARE), and LMA1 (low Mr activity 1, a heterodimer of thioredoxin and I(B)2). LMA1 requires Sec18p for saturable, high-affinity binding to vacuoles, and Sec18p "priming" ATPase requires both Sec17p and LMA1. Either the sec18-1 mutation and deletion of I(B)2, or deletion of both I(B)2 and p13 (an I(B)2 homolog) causes a striking synthetic vacuole fragmentation phenotype. Upon Sec18p ATP hydrolysis, LMA1 transfers to (and stabilizes) a Vam3p complex. LMA1 is released from vacuoles in a phosphatase-regulated reaction. This LMA1 cycle explains how priming by Sec18p is coupled to t-SNARE stabilization and to fusion."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0092-8674(00)81457-9"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0092-8674(00)81457-9"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/author | "Sato K."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/author | "Sato K."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/author | "Xu Z."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/author | "Xu Z."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/author | "Wickner W."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/author | "Wickner W."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/pages | "1125-1134"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/pages | "1125-1134"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/title | "LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/title | "LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion."xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/volume | "93"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://purl.uniprot.org/core/volume | "93"xsd:string |
http://purl.uniprot.org/citations/9657146 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9657146 |
http://purl.uniprot.org/citations/9657146 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9657146 |
http://purl.uniprot.org/citations/9657146 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9657146 |
http://purl.uniprot.org/citations/9657146 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9657146 |