α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency
Seyedeh Sahar Tahaei Gilan,1,* Dorsa Yahya Rayat,1,* Twana Ahmed Mustafa,2 Falah Mohammad Aziz,3 Koorosh Shahpasand,4 Keivan Akhtari,5 Abbas Salihi,3,6 Osama K Abou-Zied,7 Mojtaba Falahati81Department of Cellular and Molecular Biology, Faculty of Advanced Science and Technology, Tehran Medical Scien...
Guardado en:
Autores principales: | Tahaei Gilan SS, Yahya Rayat D, Mustafa TA, Aziz FM, Shahpasand K, Akhtari K, Salihi A, Abou-Zied OK, Falahati M |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Dove Medical Press
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/091d5c5a18754146ac2b7bbb88e4a329 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
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) -
Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity
por: Zand Z, et al.
Publicado: (2019) -
Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
por: Mantas Ziaunys, et al.
Publicado: (2021) -
The Small Molecule Alpha-Synuclein Aggregator, FN075, Enhances Alpha-Synuclein Pathology in Subclinical AAV Rat Models
por: Rachel Kelly, et al.
Publicado: (2021) -
Effects of the Toxic Metals Arsenite and Cadmium on α-Synuclein Aggregation In Vitro and in Cells
por: Emma Lorentzon, et al.
Publicado: (2021)