Nicastrin Functions as a γ-Secretase-Substrate Receptor
By Sanjiv J. Shah, Sheu-Fen Lee, K. Tabuchi, Yi‐Heng Hao, Cong Yu, Q. LaPlant, H. Ball, C. Dann, T. Sūdhof, Gang Yu. 2005
432 citations recorded by the source corpus.
Subfields: Cell Biology, Nutrition and Dietetics, Physiology
View Paper: https://www.semanticscholar.org/paper/bc564ace99597038e0983c0056b946682c604444
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In Physiology
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Citations in the corpus
- Trafficking and proteolytic processing of APP. (2012, background): “NCT is probably required as a sizeselecting substrate receptor (Shah et al. 2005; Dries et al. 2009), although recent findings may challenge such a function (Chavez-Gutierrez et al.”
- c-Myc is an important direct target of Notch1 in T-cell acute lymphoblastic leukemia/lymphoma. (2006, background): “In contrast, ICN1 did not associate with site B.”
- Alzheimer’s Disease and the β-Amyloid Peptide (2010, neutral): “Although the exact functional roles of each component have yet to be fully elucidated, presenilin is believed to form the active site of the aspartyl protease [16,17], and nicastrin likely serves as a substrate docking subunit [18].”
- Presenilins form ER Ca2+ leak channels, a function disrupted by familial Alzheimer's disease-linked mutations. (2006, methodology): “Recombinant baculoviruses were generated using the Bac-to-Bac system (Invitrogen) as previously described (Shah et al., 2005; Tu et al., 2005a, 2005b).”
- The Canonical Notch Signaling Pathway: Unfolding the Activation Mechanism (2009, background): “NEXT Up, Intramembrane Notch Proteolysis Even though all membrane-tethered forms of Notch can interact with γ-secretase within the secretory pathway, only molecules with a free N terminus become substrates for intramembrane proteolysis by γ-secretase (Shah et al., 2005).”