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- W1907174433 abstract "Significance Identifying factors that regulate the degradation of α-synuclein, the protein at the center of Parkinson’s disease etiology, is vital in designing therapeutic strategies. This study provides new mechanistic insights into α-synuclein clearance in the lysosome, a cellular site for proteolysis by using purified mouse lysosomes and purified lysosomal proteases. Cathepsins B and L are identified to be vital through peptide mapping by mass spectrometry. Importantly, cathepsin L degrades α-synuclein amyloid fibrils, materials associated with neurodegeneration, and, thus, changes in its activity or levels could provide a promising avenue for intervention. Additional results on the stimulatory effect of anionic phospholipids on cathepsin activity suggest that changes in lipid metabolism may also contribute to lysosomal dysfunction leading to pathogenesis." @default.
- W1907174433 created "2016-06-24" @default.
- W1907174433 creator A5006393292 @default.
- W1907174433 creator A5081301991 @default.
- W1907174433 date "2015-07-13" @default.
- W1907174433 modified "2023-10-17" @default.
- W1907174433 title "Cysteine cathepsins are essential in lysosomal degradation of α-synuclein" @default.
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- W1907174433 doi "https://doi.org/10.1073/pnas.1500937112" @default.
- W1907174433 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4522768" @default.
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- W1907174433 hasPublicationYear "2015" @default.
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