Cargando…
C-Terminal Truncated α-Synuclein Fibrils Contain Strongly Twisted β-Sheets
[Image: see text] C-terminal truncations of monomeric wild-type alpha-synuclein (henceforth WT-αS) have been shown to enhance the formation of amyloid aggregates both in vivo and in vitro and have been associated with accelerated progression of Parkinson’s disease (PD). The correlation with PD may n...
Autores principales: | Iyer, Aditya, Roeters, Steven J., Kogan, Vladimir, Woutersen, Sander, Claessens, Mireille M. A. E, Subramaniam, Vinod |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2017
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5668890/ https://www.ncbi.nlm.nih.gov/pubmed/28968082 http://dx.doi.org/10.1021/jacs.7b07403 |
Ejemplares similares
-
The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure
por: Iyer, Aditya, et al.
Publicado: (2016) -
Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy
por: Roeters, Steven J., et al.
Publicado: (2017) -
Direct Visualization of Model Membrane Remodeling by α‐Synuclein Fibrillization
por: Chaudhary, Himanshu, et al.
Publicado: (2017) -
How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids?
por: Iyer, Aditya, et al.
Publicado: (2022) -
Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism
por: van Rooijen, Bart D., et al.
Publicado: (2010)