Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models
Author:
Publisher
Oxford University Press (OUP)
Subject
Clinical Neurology
Link
http://academic.oup.com/brain/article-pdf/129/2/451/825848/awh704.pdf
Reference52 articles.
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3. Andersen PM, Nilsson P, Keranen ML, Forsgren L, Hagglund J, Karlsborg M, et al. Phenotypic heterogeneity in motor neuron disease patients with CuZn-superoxide dismutase mutations in Scandinavia. Brain1997; 120: 1723–37.
4. Andersen PM, Sims KB, Xin WW, Kiely R, O´Neill G, Ravits J, et al. Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes. Amyotroph Lateral Scler Other Motor Neuron Disord2003; 2: 62–73.
5. Arnesano F, Banci L, Bertini I, Martinelli M, Furukawa Y, O'Halloran TV. The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem2004; 279: 47998–8003.
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