Misfolding and subsequent aberrant selfassembly of certain proteins into toxic amyloid deposits are hallmarks of various diseases,most notably neurodegenerative disorders such as Alzheimer’s disease(AD)and Parkinson...Misfolding and subsequent aberrant selfassembly of certain proteins into toxic amyloid deposits are hallmarks of various diseases,most notably neurodegenerative disorders such as Alzheimer’s disease(AD)and Parkinson’s disease(Chiti and Dobson,2017).Aromatic residues in amyloidogenic proteins have been shown to be key factors in protein oligomerization and fibrilization,mostly driven byπ-πinteractions.Together with aromaticity,post-translational modifications can greatly affect a protein’s solubility and conformation and,as a consequence,its propensity to aggregate.展开更多
基金supported by the Israel Ministry of Science and the Alliance Family Trust(to DS).AP is recipient of a fellowship from the Aufzien Family Center for the Prevention and Treatment of Parkinson’s Disease(APPD)EZ has received funding from the MINDED fellowship of the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No.754490.
文摘Misfolding and subsequent aberrant selfassembly of certain proteins into toxic amyloid deposits are hallmarks of various diseases,most notably neurodegenerative disorders such as Alzheimer’s disease(AD)and Parkinson’s disease(Chiti and Dobson,2017).Aromatic residues in amyloidogenic proteins have been shown to be key factors in protein oligomerization and fibrilization,mostly driven byπ-πinteractions.Together with aromaticity,post-translational modifications can greatly affect a protein’s solubility and conformation and,as a consequence,its propensity to aggregate.
