[HTML][HTML] The seeds of neurodegeneration: prion-like spreading in ALS
M Polymenidou, DW Cleveland - Cell, 2011 - cell.com
Cell, 2011•cell.com
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 …
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 …
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.
cell.com