Phosphorylation of amyloid-beta at the serine 26 residue by human cdc2 kinase.

@article{Milton2001PhosphorylationOA,
  title={Phosphorylation of amyloid-beta at the serine 26 residue by human cdc2 kinase.},
  author={Nathaniel G. N. Milton},
  journal={Neuroreport},
  year={2001},
  volume={12 17},
  pages={3839-44}
}
The amyloid-beta (Abeta) peptide has been implicated in the pathology of Alzheimer's disease (AD). Using an antisense peptide approach a novel interaction between Abeta and the human cdc2 kinase was identified. The Abeta 1-42, 1-40 and 25-35 peptides were shown to be substrates for the cdc2 kinase and phosphorylated on the Serine 26 residue. Phosphorylated Abeta (pSAbeta) was found in extracts from NT-2 neurons and AD brain. In NT-2 neurons the levels of pSAbeta were increased in the presence… CONTINUE READING

From This Paper

Topics from this paper.
14 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

Similar Papers

Loading similar papers…