| http://purl.uniprot.org/citations/11997377 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11997377 | http://www.w3.org/2000/01/rdf-schema#comment | "Even under optimal conditions, many metabolic processes, including the chloroplastic, mitochondrial, and plasma membrane-linked electron transport systems of higher plants, produce active oxygen species (AOS). Furthermore, the imposition of biotic and abiotic stress conditions can give rise to excess concentrations of AOS, resulting in oxidative damage at the cellular level. Therefore, antioxidants and antioxidant enzymes function to interrupt the cascades of uncontrolled oxidation in each organelle. Ascorbate peroxidase (APX) exists as isoenzymes and plays an important role in the metabolism of H(2)O(2) in higher plants. APX is also found in eukaryotic algae. The characterization of APX isoenzymes and the sequence analysis of their clones have led to a number of investigations that have yielded interesting and novel information on these enzymes. Interestingly, APX isoenzymes of chloroplasts in higher plants are encoded by only one gene, and their mRNAs are generated by alternative splicing of the gene's two 3'-terminal exons. Manipulation of the expression of the enzymes involved in the AOS-scavenging systems by gene-transfer technology has provided a powerful tool for increasing the present understanding of the potential of the defence network against oxidative damage caused by environmental stresses. Transgenic plants expressing E. coli catalase to chloroplasts with increased tolerance to oxidative stress indicate that AOS-scavenging enzymes, especially chloroplastic APX isoenzymes are sensitive under oxidative stress conditions. It is clear that a high level of endogenous ascorbate is essential effectively to maintain the antioxidant system that protects plants from oxidative damage due to biotic and abiotic stresses."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.org/dc/terms/identifier | "doi:10.1093/jxb/53.372.1305"xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/author | "Ishikawa T."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/author | "Takeda T."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/author | "Yoshimura K."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/author | "Miyagawa Y."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/author | "Shigeoka S."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/author | "Yabuta Y."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/author | "Tamoi M."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/name | "J Exp Bot"xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/pages | "1305-1319"xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/title | "Regulation and function of ascorbate peroxidase isoenzymes."xsd:string |
| http://purl.uniprot.org/citations/11997377 | http://purl.uniprot.org/core/volume | "53"xsd:string |
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