The Seeds of Neurodegeneration: Prion-like Spreading in ALS | Zendy

Magdalini Polymenidou | Zendy; Don W. Cleveland | Zendy

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The Seeds of Neurodegeneration: Prion-like Spreading in ALS

Author(s) -

Magdalini Polymenidou,

Don W. Cleveland

Publication year - 2011

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2011.10.011

Subject(s) - amyotrophic lateral sclerosis , neurodegeneration , biology , mechanism (biology) , sod1 , disease , neuroscience , protein aggregation , gene isoform , protein folding , prion protein , microbiology and biotechnology , genetics , gene , medicine , pathology , philosophy , epistemology

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.

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