Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
Protein aggregate formation is linked with multiple amyloidoses, including Alzheimer‘s and Parkinson‘s diseases. Currently, the understanding of such fibrillar structure formation and propagation is still not sufficient, the outcome of which is a lack of potent, anti-amyloid drugs. The environmental...
Guardado en:
Autores principales: | Mantas Ziaunys, Andrius Sakalauskas, Kamile Mikalauskaite, Vytautas Smirnovas |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
MDPI AG
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/d66f5127a55743568622f55c7d58416f |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
The Bacterial Amyloids Phenol Soluble Modulins from <i>Staphylococcus aureus</i> Catalyze Alpha-Synuclein Aggregation
por: Caroline Haikal, et al.
Publicado: (2021) -
Gallic acid oxidation products alter the formation pathway of insulin amyloid fibrils
por: Andrius Sakalauskas, et al.
Publicado: (2020) -
The Small Molecule Alpha-Synuclein Aggregator, FN075, Enhances Alpha-Synuclein Pathology in Subclinical AAV Rat Models
por: Rachel Kelly, et al.
Publicado: (2021) -
Effect of superparamagnetic nanoparticles coated with various electric charges on α-synuclein and β-amyloid proteins fibrillation process
por: Javdani N, et al.
Publicado: (2019) -
α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency
por: Tahaei Gilan SS, et al.
Publicado: (2019)