bp(HBP:HBP00073)
Overexpression of Mint1, Mint2, or Fe65 causes reduction in Aβ generation and deposition in the brains of transgenic mice, strongly suggesting a physiological role for these adaptors in regulating APP processing in the nervous tis- sue (17). PubMed:18650430
Overexpression of Mint1, Mint2, or Fe65 causes reduction in Aβ generation and deposition in the brains of transgenic mice, strongly suggesting a physiological role for these adaptors in regulating APP processing in the nervous tis- sue (17). PubMed:18650430
Overexpression of Mint1, Mint2, or Fe65 causes reduction in Aβ generation and deposition in the brains of transgenic mice, strongly suggesting a physiological role for these adaptors in regulating APP processing in the nervous tis- sue (17). PubMed:18650430
Rab6, a member of the GTP-binding protein family of membrane trafficking regulators, is implicated in protein transport along biosynthetic and endocytic pathways and has also been found to affect APP processing PubMed:21214928
Several studies have reported that certain ligands, including Abeta, F-spondin, Nogo- 66, netrin-1 and BRI2, bind to the extracellular domain of APP, resulting in modulated APP processing and sequential downstream signals (Lorenzo et al. 2000; Lu et al. 2003b; Ho and Sudhof 2004; Park et al. 2006; Lourenco et al. 2009; Matsuda et al. 2009; Zheng and Koo 2011) PubMed:22122372
Several studies have reported that certain ligands, including Abeta, F-spondin, Nogo- 66, netrin-1 and BRI2, bind to the extracellular domain of APP, resulting in modulated APP processing and sequential downstream signals (Lorenzo et al. 2000; Lu et al. 2003b; Ho and Sudhof 2004; Park et al. 2006; Lourenco et al. 2009; Matsuda et al. 2009; Zheng and Koo 2011) PubMed:22122372
Several studies have reported that certain ligands, including Abeta, F-spondin, Nogo- 66, netrin-1 and BRI2, bind to the extracellular domain of APP, resulting in modulated APP processing and sequential downstream signals (Lorenzo et al. 2000; Lu et al. 2003b; Ho and Sudhof 2004; Park et al. 2006; Lourenco et al. 2009; Matsuda et al. 2009; Zheng and Koo 2011) PubMed:22122372
Several studies have reported that certain ligands, including Abeta, F-spondin, Nogo- 66, netrin-1 and BRI2, bind to the extracellular domain of APP, resulting in modulated APP processing and sequential downstream signals (Lorenzo et al. 2000; Lu et al. 2003b; Ho and Sudhof 2004; Park et al. 2006; Lourenco et al. 2009; Matsuda et al. 2009; Zheng and Koo 2011) PubMed:22122372
Several studies have reported that certain ligands, including Abeta, F-spondin, Nogo- 66, netrin-1 and BRI2, bind to the extracellular domain of APP, resulting in modulated APP processing and sequential downstream signals (Lorenzo et al. 2000; Lu et al. 2003b; Ho and Sudhof 2004; Park et al. 2006; Lourenco et al. 2009; Matsuda et al. 2009; Zheng and Koo 2011) PubMed:22122372
Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372
Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372
Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372
Some of these lead to an impairment of the ALN owing to reduced activation of beclin 1; another repercussion may be altered process- ing of APP, providing an unexpected link to AD 69,71–73 . PubMed:30116051
Rab6, a member of the GTP-binding protein family of membrane trafficking regulators, is implicated in protein transport along biosynthetic and endocytic pathways and has also been found to affect APP processing PubMed:21214928
Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372
Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372
Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372
Some of these lead to an impairment of the ALN owing to reduced activation of beclin 1; another repercussion may be altered process- ing of APP, providing an unexpected link to AD 69,71–73 . PubMed:30116051
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.