Characterization of the glycosylation profiles of Alzheimer's beta -secretase protein Asp-2 expressed in a variety of cell lines.

@article{Charlwood2001CharacterizationOT,
  title={Characterization of the glycosylation profiles of Alzheimer's beta -secretase protein Asp-2 expressed in a variety of cell lines.},
  author={Joanne K Charlwood and Colin Dingwall and Rosalie E Matico and Ishrut Hussain and Kyung Johanson and Sean Moore and David J Powell and John Mark Skehel and Steven Ratcliffe and Brian Clarke and John J. Trill and Sharon Sweitzer and Patrick Camilleri},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 20},
  pages={16739-48}
}
Amyloid 39-42 beta -peptides are the main components of amyloid plaques found in the brain of Alzheimer's disease patients. Amyloid 39-42 beta-peptide is formed from amyloid precursor protein by the sequential action of beta- and gamma-secretases. Asp-2 is a transmembrane aspartic protease expressed in the brain, shown to have beta-secretase activity. Mature Asp-2 has four N-glycosylation sites. In this report we have characterized the carbohydrate structures in this glycoprotein expressed in… CONTINUE READING

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