Cargando…
Tyr(682) in the Intracellular Domain of APP Regulates Amyloidogenic APP Processing In Vivo
BACKGROUND: The pathogenesis of Alzheimer's disease is attributed to misfolding of Amyloid-β (Aβ) peptides. Aβ is generated during amyloidogenic processing of Aβ-precursor protein (APP). Another characteristic of the AD brain is increased phosphorylation of APP amino acid Tyr(682). Tyr(682) is...
Autores principales: | Barbagallo, Alessia P. M., Weldon, Richard, Tamayev, Robert, Zhou, Dawang, Giliberto, Luca, Foreman, Oded, D'Adamio, Luciano |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2982846/ https://www.ncbi.nlm.nih.gov/pubmed/21103325 http://dx.doi.org/10.1371/journal.pone.0015503 |
Ejemplares similares
-
The interactome of the amyloid β precursor protein family members is shaped by phosphorylation of their intracellular domains
por: Tamayev, Robert, et al.
Publicado: (2009) -
Evidence that the Amyloid beta Precursor Protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role
por: Giliberto, Luca, et al.
Publicado: (2008) -
β - but not γ-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia
por: Tamayev, Robert, et al.
Publicado: (2012) -
β- but not γ-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia
por: Tamayev, Robert, et al.
Publicado: (2012) -
Transgenic Expression of the Amyloid-β Precursor Protein-Intracellular Domain Does Not Induce Alzheimer's Disease–Like Traits In Vivo
por: Giliberto, Luca, et al.
Publicado: (2010)