Cargando…
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy
Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1–121), composed of two protofibrils that are connected via a densely-packed interface...
Autores principales: | Guerrero-Ferreira, Ricardo, Taylor, Nicholas MI, Arteni, Ana-Andreea, Kumari, Pratibha, Mona, Daniel, Ringler, Philippe, Britschgi, Markus, Lauer, Matthias E, Makky, Ali, Verasdonck, Joeri, Riek, Roland, Melki, Ronald, Meier, Beat H, Böckmann, Anja, Bousset, Luc, Stahlberg, Henning |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6957273/ https://www.ncbi.nlm.nih.gov/pubmed/31815671 http://dx.doi.org/10.7554/eLife.48907 |
Ejemplares similares
-
Cryo-EM structure of alpha-synuclein fibrils
por: Guerrero-Ferreira, Ricardo, et al.
Publicado: (2018) -
An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials
por: Bousset, Luc, et al.
Publicado: (2016) -
Unlike Twins: An NMR Comparison of Two α-Synuclein Polymorphs Featuring Different Toxicity
por: Gath, Julia, et al.
Publicado: (2014) -
Nanomechanical properties of distinct fibrillar polymorphs of the protein α-synuclein
por: Makky, Ali, et al.
Publicado: (2016) -
Structural and functional characterization of two alpha-synuclein strains
por: Bousset, Luc, et al.
Publicado: (2013)