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http://purl.uniprot.org/citations/14988495http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14988495http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14988495http://www.w3.org/2000/01/rdf-schema#comment"The Arabidopsis genome has two similar dynamin-like proteins, ADL2a and ADL2b (76.7% identity). ADL2a is reported to be localized in chloroplasts [Kang et al. (1998) Plant Mol. Biol. 38: 437], while ADL2b functions in mitochondrial division [Arimura and Tsutsumi (2002) PROC: Natl. Acad. Sci. USA 99: 5727]. Using GFP fusion proteins, we observed both ADL2a and ADL2b in portions of mitochondria but not in chloroplasts. Furthermore, cells transformed with ADL2a and ADL2b with a defective GTPase domain had normal chloroplasts but elongated mitochondria. These results imply that both ADL2b and ADL2a are involved in the division of plant mitochondria."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pch024"xsd:string
http://purl.uniprot.org/citations/14988495http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pch024"xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Tsutsumi N."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Tsutsumi N."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Arimura S."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Arimura S."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Fujimoto M."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Fujimoto M."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Nakazono M."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Nakazono M."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Aida G.P."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/author"Aida G.P."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/pages"236-242"xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/pages"236-242"xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/title"Arabidopsis dynamin-like protein 2a (ADL2a), like ADL2b, is involved in plant mitochondrial division."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/title"Arabidopsis dynamin-like protein 2a (ADL2a), like ADL2b, is involved in plant mitochondrial division."xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/volume"45"xsd:string
http://purl.uniprot.org/citations/14988495http://purl.uniprot.org/core/volume"45"xsd:string