Inhibition of death-associated protein kinase 1 attenuates the phosphorylation and amyloidogenic processing of amyloid precursor protein.

@article{Kim2016InhibitionOD,
  title={Inhibition of death-associated protein kinase 1 attenuates the phosphorylation and amyloidogenic processing of amyloid precursor protein.},
  author={Byeong Mo Kim and Mi-Hyeon You and Chun-Hau Chen and Jaehong Suh and Rudolph E. Tanzi and Tae Ho Lee},
  journal={Human molecular genetics},
  year={2016},
  volume={25 12},
  pages={
          2498-2513
        }
}
  • Byeong Mo Kim, Mi-Hyeon You, +3 authors Tae Ho Lee
  • Published 2016 in Human molecular genetics
Extracellular deposition of amyloid-beta (Aβ) peptide, a metabolite of sequential cleavage of amyloid precursor protein (APP), is a critical step in the pathogenesis of Alzheimer's disease (AD). While death-associated protein kinase 1 (DAPK1) is highly expressed in AD brains and its genetic variants are linked to AD risk, little is known about the impact of DAPK1 on APP metabolism and Aβ generation. In this study, we demonstrated a novel effect of DAPK1 in the regulation of APP processing using… CONTINUE READING

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