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http://purl.uniprot.org/citations/21057222http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21057222http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21057222http://www.w3.org/2000/01/rdf-schema#comment"The Arabidopsis ankyrin-repeat containing protein 2A (AKR2A) was shown to be an essential molecular chaperone for the peroxisomal membrane-bound ascorbate peroxidase 3 (APX3), because the biogenesis of APX3 depends on the function of AKR2A in plant cells. AKR2A binds specifically to a sequence in APX3 that is made up of a transmembrane domain followed by a few positively charged amino acid residues; this sequence is named as AKR2A-binding sequence or ABS. Interestingly, a sequence in the chloroplast outer envelope protein 7 (OEP7) shares similar features to ABS and is able to bind specifically to AKR2A, suggesting a possibility that proteins with a sequence similar to ABS could bind to AKR2A and they are all likely ligand proteins of AKR2A. This hypothesis was supported by analyzing 5 additional proteins that contain sequences similar to ABS using the yeast two-hybrid technique. A preliminary survey in the Arabidopsis genome indicates that there are at least 500 genes encoding proteins that contain sequences similar to ABS, which raises interesting questions: are these proteins AKR2A's ligand proteins and does AKR2A play a critical role in the biogenesis of these proteins in plants?"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.org/dc/terms/identifier"doi:10.4161/psb.5.11.13714"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.org/dc/terms/identifier"doi:10.4161/psb.5.11.13714"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Shen G."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Shen G."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Kuppu S."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/author"Kuppu S."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/name"Plant Signal. Behav."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/name"Plant Signal. Behav."xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/pages"1520-1522"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/pages"1520-1522"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/title"Is AKR2A an essential molecular chaperone for a class of membrane-bound proteins in plants?"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/title"Is AKR2A an essential molecular chaperone for a class of membrane-bound proteins in plants?"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/21057222http://purl.uniprot.org/core/volume"5"xsd:string