Amyloid-beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease.

@article{Cumming2005AmyloidbetaID,
  title={Amyloid-beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease.},
  author={Robert C. Cumming and David Schubert},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2005},
  volume={19 14},
  pages={2060-2}
}
GAPDH is a redox-sensitive glycolytic enzyme that also promotes apoptosis when translocated to the nucleus and associates with aggregate-prone proteins involved in neurodegenerative disorders. Recent evidence indicates that polymorphic variation within GAPDH genes is associated with an elevated risk of developing Alzheimer's disease (AD). We previously demonstrated that GAPDH readily undergoes disulfide bonding following oxidant exposure, although the consequence of disulfide bonding on GAPDH… CONTINUE READING
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