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http://purl.uniprot.org/citations/18849574http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18849574http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18849574http://www.w3.org/2000/01/rdf-schema#comment"Sphingoid long-chain base (LCB) 1-phosphates are degradated by LCB 1-phosphate lyase to C(16) fatty aldehydes and phosphoethanolamine. Here, we confirmed that the At1g27980 gene product, AtDPL1, is a functional LCB-1-phosphate lyase. Expression of green fluorescent protein fusion products in suspension-cultured Arabidopsis cells showed that AtDPL1 is located to the endoplasmic reticulum. The rates of fresh weight decreases of dpl1-1 and dpl1-2 mutants were significantly slower than those of the wild-type plants. This ability to limit their transpiration reflected the leaf temperature of the mutant plants more than that of wild-type plants, suggesting that AtDPL1 plays a role in dehydration stress."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pcn149"xsd:string
http://purl.uniprot.org/citations/18849574http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pcn149"xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Hara-Nishimura I."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Hara-Nishimura I."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Takahashi Y."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Takahashi Y."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Tamura K."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Tamura K."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Ishiguro M."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Ishiguro M."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Imai H."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Imai H."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Hosokawa K."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Hosokawa K."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Shimazaki K."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Shimazaki K."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Nishikawa M."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Nishikawa M."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Minamioka H."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/author"Minamioka H."xsd:string
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18849574http://purl.uniprot.org/core/date"2008"xsd:gYear