Cargando…
Allosteric Modulation of PS1/γ-Secretase Conformation Correlates with Amyloid β(42/40) Ratio
BACKGROUND: Presenilin 1(PS1) is the catalytic subunit of γ-secretase, the enzyme responsible for the Aβ C-terminal cleavage site, which results in the production of Aβ peptides of various lengths. Production of longer forms of the Aβ peptide occur in patients with autosomal dominant Alzheimer disea...
Autores principales: | Uemura, Kengo, Lill, Christina M., Li, Xuejing, Peters, Jessica A., Ivanov, Alexander, Fan, Zhanyun, DeStrooper, Bart, Bacskai, Brian J., Hyman, Bradley T., Berezovska, Oksana |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2773935/ https://www.ncbi.nlm.nih.gov/pubmed/19924286 http://dx.doi.org/10.1371/journal.pone.0007893 |
Ejemplares similares
-
Substrate docking to γ-secretase allows access of γ-secretase modulators to an allosteric site
por: Uemura, Kengo, et al.
Publicado: (2010) -
The dynamic conformational landscape of γ-secretase
por: Elad, Nadav, et al.
Publicado: (2015) -
A Novel NIR-FRET Biosensor for Reporting PS/γ-Secretase Activity in Live Cells
por: Houser, Mei CQ, et al.
Publicado: (2020) -
Reciprocal relationship between APP positioning relative to the membrane and PS1 conformation
por: Uemura, Kengo, et al.
Publicado: (2011) -
Visualization of PS/γ-Secretase Activity in Living Cells
por: Maesako, Masato, et al.
Publicado: (2020)