Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State Nuclear Magnetic Resonance

Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State Nuclear Magnetic Resonance

© 2020 American Chemical Society. The microtubule-associated protein tau aggregates into distinct neurofibrillary tangles in brains afflicted with multiple neurodegenerative diseases such as Alzheimer's disease and corticobasal degeneration (CBD). The mechanism of tau misfolding and aggregation...

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Bibliographic Details
Main Authors: Dregni, Aurelio J, Duan, Pu, Hong, Mei
Other Authors: Massachusetts Institute of Technology. Department of Chemistry
Format: Article
Language:English
Published: American Chemical Society (ACS) 2022
Online Access:https://hdl.handle.net/1721.1/141074

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https://hdl.handle.net/1721.1/141074

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