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- W2119048511 abstract "Significance This study describes the nonenzymatic preparation of a protein conjugated to a tetraubiquitin Lys48-based chain made of native isopeptide bonds. We show that certain properties of our model protein, the Parkinson disease-associated protein α-Synuclein (α-Syn), are differentially regulated depending on the length of the conjugated ubiquitin (Ub) chain. In addition, we show that cross-talks between phosphorylation and ubiquitination may play important roles in regulating α-Syn aggregation and pathophysiology. The versatile synthetic strategy described here will enable future studies to further dissect the roles of Ub chain lengths and linkage types, conjugated in a site-specific manner, in regulating the physiological and pathological functions of α-Syn and other proteins." @default.
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- W2119048511 date "2013-09-16" @default.
- W2119048511 modified "2023-10-12" @default.
- W2119048511 title "Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology" @default.
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- W2119048511 doi "https://doi.org/10.1073/pnas.1315654110" @default.
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