Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

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...

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Bibliographic Details
Main Authors: Ricardo Guerrero-Ferreira, Nicholas MI Taylor, Ana-Andreea Arteni, Pratibha Kumari, Daniel Mona, Philippe Ringler, Markus Britschgi, Matthias E Lauer, Ali Makky, Joeri Verasdonck, Roland Riek, Ronald Melki, Beat H Meier, Anja Böckmann, Luc Bousset, Henning Stahlberg
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2019-12-01
Series:eLife
Subjects:
Parkinson's disease
alpha-synuclein
cryo-EM
structural biology
neurodegeneration
Online Access:https://elifesciences.org/articles/48907

Internet

https://elifesciences.org/articles/48907

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