Presenilin‐dependent γ‐secretase processing of β‐amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
By M. Sastre, H. Steiner, K. Fuchs, A. Capell, G. Multhaup, M. Condron, David B. Teplow, Christian Haass. 2001
460 citations recorded by the source corpus.
Subfields: Neurology, Oncology, Physiology
View Paper: https://www.semanticscholar.org/paper/3d913d355fb84d6888e1f374db959a03169a6c73
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In Neurology
In Physiology
- Christian Haass
- Sangram S. Sisodia
- Thomas Wisniewski
- T. Tomita
- D. Selkoe
- Huaxi Xu
- C. Kaether
- G. Thinakaran
Citations in the corpus
- Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide (2007, background): “The e-cleavage close to the cytoplasmic border of the TMD releases the free ICD into the cytoso”
- APP processing in Alzheimer's disease (2011, background): “[100,101], suggesting a sequential cleavage model where cleavage at the ε-site is followed by the ζ-site and g-site.”
- Trafficking and proteolytic processing of APP. (2012, background): “…irrelevant. g-Secretase not only liberates Ab (from C99) and p3 (from C83) but also generates the APP intracellular domain (AICD) (Gu et al. 2001; Sastre et al. 2001; Weidemann et al. 2002), which is released into the cytosol and which may have a function in nuclear signaling (Cao and Sudhof…”
- A presenilin‐1/γ‐secretase cleavage releases the E‐cadherin intracellular domain and regulates disassembly of adherens junctions (2002, background): “Recent data (Gu et al., 2001; Sastre et al., 2001; Yu et al., 2001) suggest that the APP cleavage may not occur in the middle of the transmembrane sequence of APP that de®nes the Cterminus of Ab peptides, but rather closer to the cytoplasm about three residues inside the membrane.”
- Presenilins mediate a dual intramembranous γ‐secretase cleavage of Notch‐1 (2002, background): “The cleavage, which results in the liberation of ICDs, takes place very close to the cytoplasmic border of these proteins (Schroeter et al., 1998; Gu et al., 2001; Okamoto et al., 2001; Sastre et al., 2001; Yu et al., 2001; Marambaud et al., 2002; Weidemann et al., 2002).”
- ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons (2010, methodology): “For detection of ADAM9, 10, 17 and calnexin, cell membranes were prepared as described (Sastre et al, 2001).”