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- W2016974971 abstract "By using Tb3+ as a luminescent probe, we demonstrate that the phosphorylation state of a 14-residue peptide fragment of α-synuclein, a protein implicated in Parkinson's Disease, dramatically affects the metal ion affinity of the peptide. Whereas the unphosphorylated peptide and its phosphoserine analogue show weak Tb3+ binding, its phosphotyrosine analogue shows tight 1:1 binding as well as 2:1 and 3:1 Tb:peptide adducts. Our data suggest that the phosphorylated amino acid must be appropriately positioned among additional ligating residues to establish this phosphorylation-dependent metal binding." @default.
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- W2016974971 date "2005-06-15" @default.
- W2016974971 modified "2023-09-25" @default.
- W2016974971 title "Phosphorylation of an α-Synuclein Peptide Fragment Enhances Metal Binding" @default.
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- W2016974971 doi "https://doi.org/10.1021/ja043247v" @default.
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