GAPDH is conformationally and functionally altered in association with oxidative stress in mouse models of amyotrophic lateral sclerosis.

@article{Pierce2008GAPDHIC,
  title={GAPDH is conformationally and functionally altered in association with oxidative stress in mouse models of amyotrophic lateral sclerosis.},
  author={Anson P. Pierce and Hamid Mirzaei and Florian Muller and Eric de Waal and Alexander B Taylor and Shanique Leonard and Holly van Remmen and Fred Regnier and Arlan Richardson and Asish Ray Chaudhuri},
  journal={Journal of molecular biology},
  year={2008},
  volume={382 5},
  pages={
          1195-210
        }
}
It is proposed that conformational changes induced in proteins by oxidation can lead to loss of activity or protein aggregation through exposure of hydrophobic residues and alteration in surface hydrophobicity. Because increased oxidative stress and protein aggregation are consistently observed in amyotrophic lateral sclerosis (ALS), we used a 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid (BisANS) photolabeling approach to monitor changes in protein unfolding in vivo in skeletal muscle… CONTINUE READING

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