Processing of Notch and amyloid precursor protein by γ-secretase is spatially distinct
By L. Tarassishin, Y. Yin, Bhramdeo Bassit, Yue-Ming Li. 2004
97 citations recorded by the source corpus.
Subfields: Biomaterials, Cell Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/66d10a933af6077907ca959b3122cf1098bb51e1
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In Physiology
Citations in the corpus
- APP processing in Alzheimer's disease (2011, unknown): “plasma membrane [34,36,123].”
- The Canonical Notch Signaling Pathway: Unfolding the Activation Mechanism (2009, background): “The notion that stable NICD-V is generated at the plasma membrane or in the earliest vesicles to pinch off from the plasma membrane is consistent with the observation that non-cell-permeable γ-secretase inhibitors can still block Notch proteolysis (Tarassishin et al., 2004).”
- Notch signaling: simplicity in design, versatility in function (2011, background): “…cell surface (Hansson et al., 2005), there are indications that the majority of cleavage occurs after internalization of the receptor by endocytosis (Vaccari et al., 2008), although there is also evidence to the contrary (Kaether et al., 2006; Sorensen and Conner, 2010; Tarassishin et al., 2004).”
- Trafficking and proteolytic processing of APP. (2012, methodology): “…have passed theGolgi; (4)g-secretase has been shown by various methods, including cell surface biotinylation, binding of biotinylated inhibitors specific for the active complex, and microscopic techniques, to be present at the PM (Kaether et al. 2002; Tarassishin et al. 2004; Chyung et al. 2005).”