Presenilins mediate a dual intramembranous γ‐secretase cleavage of Notch‐1
By M. Okochi, H. Steiner, Akio Fukumori, H. Tanii, T. Tomita, Toshihisa Tanaka, T. Iwatsubo, T. Kudo, M. Takeda, Christian Haass. 2002
213 citations recorded by the source corpus.
Subfields: Materials Chemistry, Oncology, Physiology
View Paper: https://www.semanticscholar.org/paper/aaf369b37fece062b8c277872474506ef8583298
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Citations in the corpus
- The Canonical Notch Signaling Pathway: Unfolding the Activation Mechanism (2009, background): “…initial cleavage at site 3 releases NICD, whereas the last cleavage at site 4 releases the Nß peptide (named after the Aß peptide, which is released from another γ-secretase substrate, amyloid precursor protein, which is associated with Alzheimer’s disease; Okochi et al., 2002) (Figures 1 and 2A).”
- Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies (2016, background): “Presenilins are also implicated in the processing of notch [104,105], an important developmental protein (mice that have PS1 knocked out die early in development from developmental abnormalities similar to those found when notch is disrupted, [106]).”