Maniecka Z Polymenidou M 2015 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. https://sonar.ch/global/documents/12733 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.virusres.2014.12.032 info:eu-repo/semantics/altIdentifier/pmid/25656065 Virus research. - 2015 ALS C9orf72 FUS Prion-like transmission Stress granules TDP-43 Amyotrophic Lateral Sclerosis Animals DNA-Binding Proteins Humans Protein Aggregation, Pathological RNA-Binding Protein FUS Superoxide Dismutase Superoxide Dismutase-1 From nucleation to widespread propagation: A prion-like concept for ALS. http://purl.org/coar/resource_type/c_6501