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- W2921940503 endingPage "261" @default.
- W2921940503 startingPage "261" @default.
- W2921940503 abstract "Increasing evidence suggests that neurodegenerative disorders share a common pathogenic feature: the presence of deposits of misfolded proteins with altered physicochemical properties in the Central Nervous System. Despite a lack of infectivity, experimental data show that the replication and propagation of neurodegenerative disease-related proteins including amyloid-β (Aβ), tau, α-synuclein and the transactive response DNA-binding protein of 43 kDa (TDP-43) share a similar pathological mechanism with prions. These observations have led to the terminology of “prion-like” to distinguish between conditions with noninfectious characteristics but similarities with the prion replication and propagation process. Prions are considered to adapt their conformation to changes in the context of the environment of replication. This process is known as either prion selection or adaptation, where a distinct conformer present in the initial prion population with higher propensity to propagate in the new environment is able to prevail over the others during the replication process. In the last years, many studies have shown that prion-like proteins share not only the prion replication paradigm but also the specific ability to aggregate in different conformations, i.e., strains, with relevant clinical, diagnostic and therapeutic implications. This review focuses on the molecular basis of the strain phenomenon in prion and prion-like proteins." @default.
- W2921940503 created "2019-03-22" @default.
- W2921940503 creator A5006285239 @default.
- W2921940503 creator A5013247323 @default.
- W2921940503 creator A5016833901 @default.
- W2921940503 creator A5025497157 @default.
- W2921940503 date "2019-03-14" @default.
- W2921940503 modified "2023-09-30" @default.
- W2921940503 title "Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration" @default.
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