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- W4385308092 abstract "The C-terminal domain of the cellular prion protein (PrPC) contains two N-linked glycosylation sites, the occupancy of which impacts disease pathology. In this study, we demonstrate that glycans at these sites are required to maintain an intramolecular interaction with the N-terminal domain, mediated through a previously identified copper-histidine tether, which suppresses the neurotoxic activity of PrPC. NMR and electron paramagnetic resonance spectroscopy demonstrate that the glycans refine the structure of the protein's interdomain interaction. Using whole-cell patch-clamp electrophysiology, we further show that cultured cells expressing PrP molecules with mutated glycosylation sites display large, spontaneous inward currents, a correlate of PrP-induced neurotoxicity. Our findings establish a structural basis for the role of N-linked glycans in maintaining a nontoxic, physiological fold of PrPC." @default.
- W4385308092 created "2023-07-28" @default.
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- W4385308092 date "2023-09-01" @default.
- W4385308092 modified "2023-10-18" @default.
- W4385308092 title "N-glycosylation is a potent regulator of prion protein neurotoxicity" @default.
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- W4385308092 doi "https://doi.org/10.1016/j.jbc.2023.105101" @default.
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