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Amyotrophic lateral sclerosis familial

Stieber, A., Gonatas, J. O., Moore, J. S. et al. Disruption of the structure of the Golgi apparatus and the function of the secretory pathway by mutants G93A and G85R of Cu, Zn superoxide dismutase (SOD1) of familial amyotrophic lateral sclerosis. /. Neurol. Sci. 219 45-53, 2004. [Pg.628]

Familial amyotrophic lateral sclerosis. Familial amyotrophic lateral sclerosis (FALS) is observed in =10% of all cases, but substantially more ALS cases are suspected to be influenced to some degree by genetic factors [75], Mutations in two genes (SOD1 and ALS2 Table 39-3) have been shown to cause FALS, apart from mutations in tau (MAPT) leading to FTD with parkinsonism and... [Pg.661]

Hosier, B. A., Siddique, T., Sapp, P. C. etal. Linkage of familial amyotrophic lateral sclerosis with frontotemporal dementia to chromosome 9q21-q22. J.A.M.A. 284 1664-1669,2000. [Pg.665]

Rosen, D. R., Siddique, T., Patterson, D. et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362 59-62, 1993. [Pg.665]

Hadano, S., Hand, C. K., Osuga, H. et al. A gene encoding a putative GTPase regulator is mutated in familial amyotrophic lateral sclerosis 2. Nat. Genet. 29 166-173, 2001. [Pg.666]

Familial-amyotrophic-lateral-sclerosis-linked mutant SOD1 mice... [Pg.731]

Borchelt, D. R., Lee, M. K., Slunt, H. H. et al. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl Acad. Sci. U.S.A. 91 8292-8296,1994. [Pg.739]

Kostic, V., Jackson-Lewis, V., de Bilbao, F., Dubois-Dauphin, M. and Przedborski, S. Bcl-2 prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis. Science 277 559-562,1997. [Pg.741]

Bowling, A. C., Barkowski, E. E., McKenna-Yasek, D. et al. Superoxide dismutase concentration and activity in familial amyotrophic lateral sclerosis. /. Neurochem. 64 2366-2369, 1995. [Pg.741]

Turner, B. J., Lopes, E. C. and Cheema, S. S. Neuromuscular accumulation of mutant superoxide dismutase 1 aggregates in a transgenic mouse model of familial amyotrophic lateral sclerosis. Neurosci. Lett. 350 132-136, 2003. [Pg.743]

Johnston, J. A., et al.. Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA, 2000, 97(23), 12571-6. [Pg.94]

Familial amyotrophic lateral sclerosis, superoxide dismutase and, 45 148 Fano resonance, 35 349-350 Fast atom bombardment mass spectrometry, heteronuclear gold cluster compounds, 39 340-342... [Pg.99]

Calabrese V. 2007. Highlight commentary on Redox proteomics analysis of oxidatively 3 modified proteins in G93A-SOD1 transgenic mice-A model of 4 familial amyotrophic lateral sclerosis. Free Radical Biol Med 43 160-162. [Pg.444]

Tortarolo M., Veglianese P., Calvaresi N., Botturi A., Rossi C., Giorgini A., Migheli A., and Bendotti C. (2003). Persistent activation of p38 mitogen-activated protein kinase in a mouse model of familial amyotrophic lateral sclerosis correlates with disease progression. Mol. Cell. Neurosci. 23 180-192. [Pg.201]

Perluigi M., Poon H. F., Hensley K., Pierce W. M., Klein J. B., Calabrese V., De Marco C., and Butterfield D. A. (2005). Proteomic analysis of 4-hydroxy-2-nonenal-modified proteins in G93A-SOD1 transgenic mice - A model of familial amyotrophic lateral sclerosis. Free Radical Biol. Med. 38 960-968. [Pg.277]

Yoshihara T, Ishigaki S, Yamamoto M, Liang Y, Niwa J, Takeuchi H, et al. Differential expression of inflammation- and apoptosis-related genes in spinal cords of a mutant SOD1 transgenic mouse model of familial amyotrophic lateral sclerosis. J Neurochem 2002 80(1) 158—167. [Pg.289]


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See also in sourсe #XX -- [ Pg.314 , Pg.318 , Pg.319 , Pg.320 , Pg.326 ]




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Familial amyotrophic lateral sclerosis FALS)

Lateral sclerosis

Sclerosis

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