Cargando…
Assessment of the efficacy of different procedures that remove and disassemble alpha-synuclein, tau and A-beta fibrils from laboratory material and surfaces
α-synuclein fibrillar polymorphs, Tau and Aß 1–42 fibrillar assemblies have been shown to propagate, amplify and trigger the formation of protein deposits reminiscent of those present within the central nervous system of patients developing synucleinopathies, tauopathies and amyloid plaques after in...
Autores principales: | Fenyi, Alexis, Coens, Audrey, Bellande, Tracy, Melki, Ronald, Bousset, Luc |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6050226/ https://www.ncbi.nlm.nih.gov/pubmed/30018327 http://dx.doi.org/10.1038/s41598-018-28856-2 |
Ejemplares similares
-
An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials
por: Bousset, Luc, et al.
Publicado: (2016) -
Absence of Uptake and Prion-Like Spreading of Alpha-Synuclein and Tau After Intravitreal Injection of Preformed Fibrils
por: Veys, Lien, et al.
Publicado: (2021) -
The differential solvent exposure of N-terminal residues provides “fingerprints” of alpha-synuclein fibrillar polymorphs
por: Landureau, Maud, et al.
Publicado: (2021) -
Tunneling nanotube (TNT)-mediated neuron-to neuron transfer of pathological Tau protein assemblies
por: Tardivel, Meryem, et al.
Publicado: (2016) -
α-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane
por: Monsellier, Elodie, et al.
Publicado: (2016)