NOX enzymes and the biology of reactive oxygen
Author:
Publisher
Springer Science and Business Media LLC
Subject
Energy Engineering and Power Technology,Fuel Technology
Link
http://www.nature.com/articles/nri1312.pdf
Reference69 articles.
1. McCord, J. M. & Fridovich, I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049–6055 (1969). The authors describe the discovery of superoxide dismutase and provide an elegant example of the value of basic, rather than disease-oriented, investigations in making fundamentally important discoveries with widespread implications in normal biology and pathology.
2. Melov, S. et al. Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics. J. Neurosci. 21, 8348–8353 (2001).
3. Suh, Y. -A. et al. Cell transformation by the superoxide-generating oxidase Mox1. Nature 401, 79–82 (1999). This paper describes the discovery of the first homologue of NADPH oxidase (NOX), NOX1 (originally known as MOX1), and its expression. The article, which proposed a growth-regulatory role for NOX1, has stimulated investigations into the role of NOX enzymes in cardiovascular disease and cancer.
4. Lambeth, J. D., Cheng, G., Arnold, R. S. & Edens, W. E. Novel homologs of gp91phox. Trends Biochem. Sci. 25, 459–461 (2000).
5. Babior, B. M., Lambeth, J. D. & Nauseef, W. The neutrophil NADPH oxidase. Arch. Biochem. Biophys. 397, 342–344 (2002).
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