Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis.

@article{Watanabe2007IncreasedAF,
  title={Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis.},
  author={Shohei Watanabe and Seiichi Nagano and James A Duce and Mahmoud Kiaei and Qiao-xin Li and Stephanie M. Tucker and Ashutosh Tiwari and R. H. Brown and M. Flint Beal and Lawrence J. Hayward and Valeria C Culotta and Satoshi Yoshihara and Saburo Sakoda and Ashley I. Bush},
  journal={Free radical biology & medicine},
  year={2007},
  volume={42 10},
  pages={
          1534-42
        }
}
Mutations in Cu,Zn-superoxide dismutase (SOD1) cause familial amyotrophic lateral sclerosis (ALS). It has been proposed that neuronal cell death might occur due to inappropriately increased Cu interaction with mutant SOD1. Using Cu immobilized metal-affinity chromatography (IMAC), we showed that mutant SOD1 (A4V, G85R, and G93A) expressed in transfected COS7 cells, transgenic mouse spinal cord tissue, and transformed yeast possessed higher affinity for Cu than wild-type SOD1. Serine… CONTINUE READING
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