Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants
<p>Abstract</p> <p>Background</p> <p>Amyloid precursor protein (APP) is enzymatically cleaved by γ-secretase to form two peptide products, either Aβ40 or the more neurotoxic Aβ42. The Aβ42/40 ratio is increased in many cases of familial Alzheimer's disease (FAD). T...
Main Authors: | Fraser Paul E, McLaurin Joanne, Melnyk Roman A, Guo Meng, Kim Sanguk, Gorman Paul M, Bowie James U, Chakrabartty Avijit |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2008-01-01
|
Series: | BMC Neuroscience |
Online Access: | http://www.biomedcentral.com/1471-2202/9/17 |
Similar Items
-
Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding
by: McLaurin JoAnne, et al.
Published: (2007-05-01) -
Potential Role of Venular Amyloid in Alzheimer’s Disease Pathogenesis
by: Christopher D. Morrone, et al.
Published: (2020-03-01) -
Structural Characterization of the Amyloid Precursor Protein Transmembrane Domain and Its γ‑Cleavage Site
by: Anna Itkin, et al.
Published: (2017-10-01) -
The effect of sequence and environment on the structure and dimerization of amyloid precursor protein
by: Foster, Leigh Suzanne Holmes
Published: (2016) -
Reducing amyloid beta peptide production through regulation of amyloid precursor protein dimerization
by: Meguerian, Arman
Published: (2016)