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- W4386008085 endingPage "102678" @default.
- W4386008085 startingPage "102678" @default.
- W4386008085 abstract "Neurodegenerative diseases are associated with the pathological deposition of many different intrinsically disordered proteins or proteins with intrinsically disordered regions. Recent evidence suggests that these proteins can undergo liquid-liquid phase separation and also form membrane-less organelles in cells. Additionally, the biomolecular condensates formed by these proteins may undergo liquid-to-solid phase transition thereby maturating to amyloid fibrils, oligomeric species, or amorphous aggregates and contributing to the pathology of several neurodegenerative diseases. Here we discuss the role of phase separation of the neuronal proteins tau, α-synuclein, fused in sarcoma (FUS), and the transactive response DNA-binding protein of 43 kDa (TDP-43) that are associated with neurodegeneration in the context of pathological protein aggregation." @default.
- W4386008085 created "2023-08-20" @default.
- W4386008085 creator A5000141400 @default.
- W4386008085 creator A5033249566 @default.
- W4386008085 date "2023-10-01" @default.
- W4386008085 modified "2023-10-07" @default.
- W4386008085 title "Role of aberrant phase separation in pathological protein aggregation" @default.
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- W4386008085 doi "https://doi.org/10.1016/j.sbi.2023.102678" @default.
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