Article
Alteration of familial ALS-linked mutant SOD1 solubility with disease progression: its modulation by the proteasome and Hsp70.
Biochemical and biophysical research communications - 12 May 2006
Koyama Shingo, Arawaka Shigeki, Chang-Hong Ren, Wada Manabu, Kawanami Toru, Kurita Keiji, Kato Masaaki, Nagai Makiko, Aoki Masashi, Itoyama Yasuto, Sobue Gen, Chan Pak H, Kato Takeo
Abstract excerpt
Accumulation of misfolded Cu/Zn superoxide dismutase (SOD1) occurs in patients with a subgroup of familial amyotrophic lateral sclerosis (fALS). To identify the conversion of SOD1 from a normally soluble form to insoluble aggregates, we investigated the change of SOD1 solubility with aging in fALS-linked H46R SOD1 transgenic mice. Mutant SOD1 specifically altered to insoluble forms, which were sequentially...
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