Cargando…
α-synuclein-lanthanide metal ions interaction: binding sites, conformation and fibrillation
BACKGROUND: The pathological hallmark of Parkinson’s disease is the deposition of cytoplasmic neuronal inclusions termed Lewy bodies. The major component of Lewy bodies is amyloid fibrils of α-synuclein. To investigate what causes α-synuclein aggregation is essential to understand its pathological r...
Autores principales: | Bai, Jia, Zhang, Zeting, Liu, Maili, Li, Conggang |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4739322/ https://www.ncbi.nlm.nih.gov/pubmed/26843956 http://dx.doi.org/10.1186/s13628-016-0026-1 |
Ejemplares similares
-
C-terminal truncation modulates α-Synuclein’s cytotoxicity and aggregation by promoting the interactions with membrane and chaperone
por: Zhang, Cai, et al.
Publicado: (2022) -
Metal ions shape α-synuclein
por: Moons, Rani, et al.
Publicado: (2020) -
Bivalent metal ions induce formation of α-synuclein fibril polymorphs with different cytotoxicities
por: Atarod, Deyhim, et al.
Publicado: (2022) -
Polypeptides derived from α-Synuclein binding partners to prevent α-Synuclein fibrils interaction with and take-up by cells
por: Monsellier, Elodie, et al.
Publicado: (2020) -
The hot sites of α-synuclein in amyloid fibril formation
por: Khammari, Anahita, et al.
Publicado: (2020)