期刊
VIRUS RESEARCH
卷 207, 期 -, 页码 94-105出版社
ELSEVIER
DOI: 10.1016/j.virusres.2014.12.032
关键词
ALS; Prion-like transmission; Stress granules; TDP-43; FUS; C9orf72
类别
资金
- Candoc fellowship (Forschungskredit) from University of Zurich
- Swiss National Science Foundation
- Human Frontier Science Program
- Clinical Research Priority Program Small RNAs of the University of Zurich
Propagation of pathological protein assemblies via a prion-like mechanism has been suggested to drive neurodegenerative diseases, such as Parkinson's and Alzheimer's. Recently, amyotrophic lateral sclerosis (ALS)-linked proteins, such as SOD1, TDP-43 and FUS were shown to follow self-perpetuating seeded aggregation, thereby adding ALS to the group of prion-like disorders. The cell-to-cell spread of these pathological protein assemblies and their pathogenic mechanism is poorly understood. However, as ALS is a non-cell autonomous disease and pathology in glial cells was shown to contribute to motor neuron damage, spreading mechanisms are likely to underlie disease progression via the interplay between affected neurons and their neighboring glial cells. (C) 2015 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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