The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Superoxide Dismutase in Arabidopsis: An Eclectic Enzyme Family with Disparate Regulation and Protein Localization
Open accessAbstract
A number of environmental stresses can lead to enhanced production of superoxide within plant tissues, and plants are believed to rely on the enzyme superoxide dismutase (SOD) to detoxify this reactive oxygen species. We have identified seven cDNAs and genes for SOD in Arabidopsis. These consist of three CuZnSODs (CSD1,CSD2, and CSD3), three FeSODs (FSD1, FSD2, and FSD3), and one MnSOD (MSD1). The chromosomal location of these seven SOD genes has been established. To study this enzyme family, antibodies were generated against five proteins: CSD1, CSD2, CSD3, FSD1, and MSD1. Using these antisera and nondenaturing-polyacrylamide gel electrophoresis enzyme assays, we identified protein and activity for two CuZnSODs and for FeSOD and MnSOD in Arabidopsis rosette tissue. Additionally, subcellular fractionation studies revealed the presence of CSD2 and FeSOD protein within Arabidopsis chloroplasts. The seven SOD mRNAs and the four proteins identified were differentially regulated in response to various light regimes, ozone fumigation, and ultraviolet-B irradiation. To our knowledge, this is the first report of a large-scale analysis of the regulation of multiple SOD proteins in a plant species.
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Cites
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
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[1] Role of free radicals and catalytic metal ions in human disease: An overview
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Cited by
Role of superoxide dismutases (SODs) in controlling oxidative stress in plants
Alscher, R. G. (2002) · Journal of Experimental Botany · doi:10.1093/jexbot/53.372.1331 · Cited by 2,771
Sunkar, R., Kapoor, A., & Zhu, J.-K. (2006) · The Plant Cell · doi:10.1105/tpc.106.041673 · Cited by 1,313
Harb, A., Krishnan, A., Ambavaram, M. M. R., & Pereira, A. (2010) · Plant Physiology · doi:10.1104/pp.110.161752 · Cited by 747
The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation
Palenik, B., Grimwood, J., Aerts, A., Rouzé, P., Salamov, A., Putnam, N., Dupont, C., Jorgensen, R., Derelle, E., Rombauts, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611046104 · Cited by 625
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Metadata
- Authors
- Kliebenstein, D. J., Monde, R.-A., & Last, R. L.
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 1998-10-01
- Volume
- 118
- Issue
- 2
- Pages
- 637-650
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- OpenAlex
- W2148951714
- Cited by
- 630
- References
- 4
- FWCI
- 13.94
- Type
- journal article
- Language
- en
- Open access
- green
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- Kliebenstein, D. J., Monde, R.-A., & Last, R. L. (1998). Superoxide Dismutase in Arabidopsis: An Eclectic Enzyme Family with Disparate Regulation and Protein Localization. Plant Physiology. https://doi.org/10.1104/pp.118.2.637
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