Abstract：
:Misfolded proteins accumulating in several neurodegenerative diseases (including Alzheimer, Parkinson, and Huntington diseases) can cause aggregation of their native counterparts through a mechanism similar to the infectious prion protein's induction of a pathogenic conformation onto its cellular isoform. Evidence for such a prion-like mechanism has now spread to the main misfolded proteins, SOD1 and TDP-43, implicated in amyotrophic lateral sclerosis (ALS). The major neurodegenerative diseases may therefore have mechanistic parallels for non-cell-autonomous spread of disease within the nervous system.
journal_name
Celljournal_title
Cellauthors
Polymenidou M,Cleveland DWdoi
10.1016/j.cell.2011.10.011subject
Has Abstractpub_date
2011-10-28 00:00:00pages
498-508issue
3eissn
0092-8674issn
1097-4172pii
S0092-8674(11)01209-8journal_volume
147pub_type
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