Cargando…
Structural Heterogeneity in Transmembrane Amyloid Precursor Protein Homodimer Is a Consequence of Environmental Selection
[Image: see text] The 99 amino acid C-terminal fragment of amyloid precursor protein (C99), consisting of a single transmembrane (TM) helix, is known to form homodimers. Homodimers can be processed by γ-secretase to produce amyloid-β (Aβ) protein, which is implicated in Alzheimer’s disease (AD). Whi...
Autores principales: | Dominguez, Laura, Foster, Leigh, Meredith, Stephen C., Straub, John E., Thirumalai, D. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4105063/ https://www.ncbi.nlm.nih.gov/pubmed/24926593 http://dx.doi.org/10.1021/ja503150x |
Ejemplares similares
-
Formation of extramembrane β-strands controls dimerization of transmembrane helices in amyloid precursor protein C99
por: Pantelopulos, George A., et al.
Publicado: (2022) -
Structural and Dynamic Study of the Transmembrane Domain of the Amyloid Precursor Protein
por: Nadezhdin, K.D., et al.
Publicado: (2011) -
Structural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains
por: Deatherage, Catherine L., et al.
Publicado: (2017) -
Cholesterol twists the transmembrane Di-Gly region of amyloid-precursor protein
por: Wang, David Tzu-Wei, et al.
Publicado: (2023) -
Mapping the Homodimer Interface of an Optimized, Artificial, Transmembrane Protein Activator of the Human Erythropoietin Receptor
por: Cohen, Emily B., et al.
Publicado: (2014)