γ-secretase processing of APLP1 leads to the production of a p3-like peptide that does not aggregate and is not toxic to neurons

@article{Minogue2009secretasePO,
  title={γ-secretase processing of APLP1 leads to the production of a p3-like peptide that does not aggregate and is not toxic to neurons},
  author={Aed{\'i}n M. Minogue and Adam K. Stubbs and Carlo Sala Frigerio and Barry Boland and Dominic M Walsh},
  journal={Brain Research},
  year={2009},
  volume={1262},
  pages={89-99}
}
  • Aedín M. Minogue, Adam K. Stubbs, +2 authors Dominic M Walsh
  • Published in Brain Research 2009
  • Biology, Medicine
  • The amyloid precursor-like protein-1 (APLP1) is a member of a protein family that includes the Alzheimer's disease-associated amyloid precursor protein (APP). While much is known about the proteolytic processing of APP, fewer details are available about APLP1. Using Chinese hamster ovarian cells stably transfected with human APLP1 and a novel juxtamembrane anti-APLP1 antibody, we demonstrate the detection of a secreted approximately 3.5 kDa APLP1-derived peptide (ALP-1). The production of this… CONTINUE READING

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